Potential of chicken by-products as sources of useful biological resources
By-products from different animal sources are currently being utilised for beneficial purposes. Chicken processing plants all over the world generate large amount of solid by-products in form of heads, legs, bones, viscera and feather. These wastes are often processed into livestock feed, fertilizer...
Saved in:
Published in | Waste management (Elmsford) Vol. 33; no. 3; pp. 552 - 565 |
---|---|
Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Ltd
01.03.2013
|
Subjects | |
Online Access | Get full text |
ISSN | 0956-053X 1879-2456 1879-2456 |
DOI | 10.1016/j.wasman.2012.08.001 |
Cover
Abstract | By-products from different animal sources are currently being utilised for beneficial purposes. Chicken processing plants all over the world generate large amount of solid by-products in form of heads, legs, bones, viscera and feather. These wastes are often processed into livestock feed, fertilizers and pet foods or totally discarded. Inappropriate disposal of these wastes causes environmental pollution, diseases and loss of useful biological resources like protein, enzymes and lipids. Utilisation methods that make use of these biological components for producing value added products rather than the direct use of the actual waste material might be another viable option for dealing with these wastes. This line of thought has consequently led to researches on these wastes as sources of protein hydrolysates, enzymes and polyunsaturated fatty acids. Due to the multi-applications of protein hydrolysates in various branches of science and industry, and the large body of literature reporting the conversion of animal wastes to hydrolysates, a large section of this review was devoted to this subject. Thus, this review reports the known functional and bioactive properties of hydrolysates derived from chicken by-products as well their utilisation as source of peptone in microbiological media. Methods of producing these hydrolysates including their microbiological safety are discussed. Based on the few references available in the literature, the potential of some chicken by-product as sources of proteases and polyunsaturated fatty acids are pointed out along with some other future applications. |
---|---|
AbstractList | By-products from different animal sources are currently being utilised for beneficial purposes. Chicken processing plants all over the world generate large amount of solid by-products in form of heads, legs, bones, viscera and feather. These wastes are often processed into livestock feed, fertilizers and pet foods or totally discarded. Inappropriate disposal of these wastes causes environmental pollution, diseases and loss of useful biological resources like protein, enzymes and lipids. Utilisation methods that make use of these biological components for producing value added products rather than the direct use of the actual waste material might be another viable option for dealing with these wastes. This line of thought has consequently led to researches on these wastes as sources of protein hydrolysates, enzymes and polyunsaturated fatty acids. Due to the multi-applications of protein hydrolysates in various branches of science and industry, and the large body of literature reporting the conversion of animal wastes to hydrolysates, a large section of this review was devoted to this subject. Thus, this review reports the known functional and bioactive properties of hydrolysates derived from chicken by-products as well their utilisation as source of peptone in microbiological media. Methods of producing these hydrolysates including their microbiological safety are discussed. Based on the few references available in the literature, the potential of some chicken by-product as sources of proteases and polyunsaturated fatty acids are pointed out along with some other future applications.By-products from different animal sources are currently being utilised for beneficial purposes. Chicken processing plants all over the world generate large amount of solid by-products in form of heads, legs, bones, viscera and feather. These wastes are often processed into livestock feed, fertilizers and pet foods or totally discarded. Inappropriate disposal of these wastes causes environmental pollution, diseases and loss of useful biological resources like protein, enzymes and lipids. Utilisation methods that make use of these biological components for producing value added products rather than the direct use of the actual waste material might be another viable option for dealing with these wastes. This line of thought has consequently led to researches on these wastes as sources of protein hydrolysates, enzymes and polyunsaturated fatty acids. Due to the multi-applications of protein hydrolysates in various branches of science and industry, and the large body of literature reporting the conversion of animal wastes to hydrolysates, a large section of this review was devoted to this subject. Thus, this review reports the known functional and bioactive properties of hydrolysates derived from chicken by-products as well their utilisation as source of peptone in microbiological media. Methods of producing these hydrolysates including their microbiological safety are discussed. Based on the few references available in the literature, the potential of some chicken by-product as sources of proteases and polyunsaturated fatty acids are pointed out along with some other future applications. By-products from different animal sources are currently being utilised for beneficial purposes. Chicken processing plants all over the world generate large amount of solid by-products in form of heads, legs, bones, viscera and feather. These wastes are often processed into livestock feed, fertilizers and pet foods or totally discarded. Inappropriate disposal of these wastes causes environmental pollution, diseases and loss of useful biological resources like protein, enzymes and lipids. Utilisation methods that make use of these biological components for producing value added products rather than the direct use of the actual waste material might be another viable option for dealing with these wastes. This line of thought has consequently led to researches on these wastes as sources of protein hydrolysates, enzymes and polyunsaturated fatty acids. Due to the multi-applications of protein hydrolysates in various branches of science and industry, and the large body of literature reporting the conversion of animal wastes to hydrolysates, a large section of this review was devoted to this subject. Thus, this review reports the known functional and bioactive properties of hydrolysates derived from chicken by-products as well their utilisation as source of peptone in microbiological media. Methods of producing these hydrolysates including their microbiological safety are discussed. Based on the few references available in the literature, the potential of some chicken by-product as sources of proteases and polyunsaturated fatty acids are pointed out along with some other future applications. |
Author | Abu Bakar, Fatimah Hashim, Dzulkifly Lasekan, Adeseye |
Author_xml | – sequence: 1 givenname: Adeseye surname: Lasekan fullname: Lasekan, Adeseye organization: Faculty of Food Science and Technology, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia – sequence: 2 givenname: Fatimah surname: Abu Bakar fullname: Abu Bakar, Fatimah email: fatim@putra.upm.edu.my organization: Faculty of Food Science and Technology, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia – sequence: 3 givenname: Dzulkifly surname: Hashim fullname: Hashim, Dzulkifly organization: Faculty of Food Science and Technology, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/22985619$$D View this record in MEDLINE/PubMed https://www.osti.gov/biblio/22439949$$D View this record in Osti.gov |
BookMark | eNqFkTFv1TAUhS1URF8L_wChSCwsCb6249gMSKiiBVQJBpDYLMe5oX7k2cV2QP33JMrrwkAnD_6-I_ucM3ISYkBCngNtgIJ8vW_-2HywoWEUWENVQyk8IjtQna6ZaOUJ2VHdypq2_PspOct5vwBCAX1CThnTqpWgd-TTl1gwFG-nKo6Vu_HuJ4aqv6tvUxxmV3Jlc5XjnBzmlZgzjvNU9T5O8Yd3i5bweP2UPB7tlPHZ8Twn3y7ff734UF9_vvp48e66dkLpUoPkOGptmdNyZAJaSt1gWylgpK2QXA3Mchha7B0Cl7SzChWKHvgwiA40Pycvt9yYizfZ-YLuxsUQ0BXDmOBai5V6tVHLR37NmIs5-OxwmmzAOGcDHVDGqVTdwygH0VElJCzoiyM69wcczG3yB5vuzH2hC_BmA1yKOScczfI-W3wMJVk_GaBmXc_szbaeWdczVJllnEUW_8j3-Q9obzcNl9Z_e0xrKRgcDj6tnQzR_z_gL6BxtFA |
CitedBy_id | crossref_primary_10_1002_jctb_6131 crossref_primary_10_1016_j_indcrop_2014_12_054 crossref_primary_10_1016_j_bcab_2017_04_004 crossref_primary_10_1016_j_tifs_2016_03_006 crossref_primary_10_1007_s12649_021_01372_7 crossref_primary_10_1016_j_jclepro_2020_121129 crossref_primary_10_1016_j_ijbiomac_2020_03_032 crossref_primary_10_1016_j_csbj_2021_11_027 crossref_primary_10_1016_j_foodchem_2021_129868 crossref_primary_10_1590_fst_03222 crossref_primary_10_1016_j_psj_2023_102791 crossref_primary_10_3390_app14198703 crossref_primary_10_1007_s13205_017_0739_0 crossref_primary_10_1093_jas_skad289 crossref_primary_10_1016_j_ijbiomac_2019_08_062 crossref_primary_10_47836_ifrj_29_5_10 crossref_primary_10_1007_s00253_015_7278_6 crossref_primary_10_1007_s12649_022_01713_0 crossref_primary_10_1111_anu_13141 crossref_primary_10_1007_s10098_018_1498_2 crossref_primary_10_1016_j_jcomc_2020_100080 crossref_primary_10_31073_foodresources2022_19_06 crossref_primary_10_1080_10601325_2014_967108 crossref_primary_10_1007_s00449_017_1737_7 crossref_primary_10_1007_s12649_023_02192_7 crossref_primary_10_1590_0103_8478cr20220444 crossref_primary_10_25130_tjes_30_1_10 crossref_primary_10_12688_f1000research_17134_2 crossref_primary_10_12688_f1000research_17134_1 crossref_primary_10_1016_j_ultsonch_2024_107165 crossref_primary_10_1016_j_mex_2019_06_002 crossref_primary_10_1111_1541_4337_12651 crossref_primary_10_1016_j_fbio_2023_102935 crossref_primary_10_3390_nu10091295 crossref_primary_10_1016_j_wasman_2022_07_021 crossref_primary_10_1002_cnl2_132 crossref_primary_10_2166_wst_2020_025 crossref_primary_10_3390_polym7030580 crossref_primary_10_1016_j_tifs_2016_11_014 crossref_primary_10_1007_s10529_015_2016_9 crossref_primary_10_1002_cben_202400014 crossref_primary_10_1088_1757_899X_454_1_012190 crossref_primary_10_3389_fbioe_2019_00110 crossref_primary_10_1007_s12010_021_03554_4 crossref_primary_10_12688_f1000research_17134_3 crossref_primary_10_1016_j_jfoodeng_2015_08_003 crossref_primary_10_1016_j_aqrep_2023_101623 crossref_primary_10_1016_j_fuproc_2015_08_014 crossref_primary_10_1177_20412479211008746 crossref_primary_10_1016_j_resconrec_2022_106315 crossref_primary_10_1155_2018_6729490 crossref_primary_10_3390_polym10020176 crossref_primary_10_3390_foods12203814 crossref_primary_10_5650_jos_ess19338 crossref_primary_10_1007_s10989_019_09879_3 crossref_primary_10_1016_j_foodchem_2022_132201 crossref_primary_10_3390_ani14081203 crossref_primary_10_1016_j_ijbiomac_2020_03_116 crossref_primary_10_22207_JPAM_15_2_17 crossref_primary_10_1016_j_lwt_2021_112092 crossref_primary_10_3382_ps_pex237 crossref_primary_10_1016_j_foodchem_2024_142641 crossref_primary_10_1007_s12649_022_01947_y crossref_primary_10_1016_j_ijbiomac_2018_01_037 crossref_primary_10_1016_j_anifeedsci_2019_114226 crossref_primary_10_48165_ijapm_2023_37_2_11 crossref_primary_10_1016_j_fufo_2023_100238 crossref_primary_10_1016_j_jclepro_2022_131653 crossref_primary_10_1080_19476337_2018_1529061 crossref_primary_10_1080_12298093_2022_2059889 crossref_primary_10_3390_app12031327 crossref_primary_10_1007_s11274_016_2177_2 crossref_primary_10_3390_ani14182715 crossref_primary_10_1016_j_fbio_2024_104644 crossref_primary_10_1080_10942912_2021_1986522 crossref_primary_10_1155_2019_9105605 crossref_primary_10_3390_su151914201 crossref_primary_10_1016_j_tifs_2019_08_002 crossref_primary_10_1007_s43555_024_00038_4 crossref_primary_10_1016_j_jenvman_2021_112040 crossref_primary_10_3390_su142416764 crossref_primary_10_1007_s11756_021_00724_x crossref_primary_10_1016_j_wasman_2013_09_010 crossref_primary_10_3390_su131910837 crossref_primary_10_1021_acssusresmgt_4c00075 crossref_primary_10_3390_ijerph191710858 crossref_primary_10_1016_j_aqrep_2023_101712 crossref_primary_10_1021_acsomega_3c04417 crossref_primary_10_1007_s13399_024_05679_y crossref_primary_10_1016_j_procbio_2021_07_014 crossref_primary_10_1111_jtxs_12734 crossref_primary_10_3382_ps_pew242 crossref_primary_10_1016_j_jclepro_2020_123219 crossref_primary_10_1007_s12649_022_01801_1 crossref_primary_10_1007_s12649_021_01464_4 crossref_primary_10_3390_fermentation7030190 crossref_primary_10_1007_s11356_017_9876_6 crossref_primary_10_1016_j_rser_2017_09_007 crossref_primary_10_1016_j_crfs_2022_01_027 crossref_primary_10_3390_molecules26175280 crossref_primary_10_1016_j_clcb_2024_100119 crossref_primary_10_1002_jctb_4900 crossref_primary_10_1007_s12649_015_9368_1 crossref_primary_10_1016_j_eurpolymj_2024_113557 crossref_primary_10_1007_s10123_019_00090_4 crossref_primary_10_1111_are_15132 crossref_primary_10_1007_s12161_017_1095_8 crossref_primary_10_3390_environments10080137 crossref_primary_10_1080_15440478_2024_2346803 crossref_primary_10_1002_mnfr_201801176 crossref_primary_10_1016_j_foodchem_2020_128417 crossref_primary_10_1016_j_cjche_2015_11_007 crossref_primary_10_1111_are_14715 crossref_primary_10_3390_antiox13030305 crossref_primary_10_2478_pjct_2019_0030 crossref_primary_10_1016_j_foodres_2015_04_005 crossref_primary_10_1016_j_foodhyd_2016_09_029 crossref_primary_10_1016_j_agee_2020_107046 crossref_primary_10_1111_jfbc_12494 crossref_primary_10_3390_fermentation7030122 crossref_primary_10_1016_j_wasman_2019_06_040 crossref_primary_10_3390_fishes10020042 crossref_primary_10_1007_s12649_017_0004_0 crossref_primary_10_1007_s11356_020_10855_4 crossref_primary_10_1039_C4RA15469J crossref_primary_10_1016_j_psj_2025_105098 crossref_primary_10_1007_s11274_019_2696_8 crossref_primary_10_1007_s12649_016_9694_y crossref_primary_10_1111_anu_12665 crossref_primary_10_1016_j_jff_2019_02_006 crossref_primary_10_1021_acsomega_2c04216 crossref_primary_10_1007_s13205_016_0370_5 crossref_primary_10_1080_10942912_2017_1396477 crossref_primary_10_1007_s13399_022_02352_0 crossref_primary_10_1002_jssc_201700883 crossref_primary_10_1016_j_aqrep_2024_101990 crossref_primary_10_1016_j_fbio_2017_07_009 crossref_primary_10_1039_C9FO00695H crossref_primary_10_1016_j_foodres_2015_01_015 crossref_primary_10_1007_s12649_020_01007_3 crossref_primary_10_3390_su12051725 crossref_primary_10_5219_1786 crossref_primary_10_21323_2414_438X_2021_6_3_210_218 crossref_primary_10_3390_ani15010080 crossref_primary_10_1080_1828051X_2020_1767000 crossref_primary_10_3390_ijerph17249162 crossref_primary_10_3390_pr8111415 crossref_primary_10_1016_j_biombioe_2013_07_013 crossref_primary_10_1016_j_procbio_2024_07_023 crossref_primary_10_3390_plants12152837 crossref_primary_10_1007_s11274_023_03836_5 crossref_primary_10_31073_foodresources2024_22_01 crossref_primary_10_1016_j_resconrec_2023_106963 crossref_primary_10_1016_j_wasman_2015_05_023 crossref_primary_10_3382_ps_pey175 crossref_primary_10_1111_lam_13428 crossref_primary_10_1002_jsfa_12802 crossref_primary_10_1002_fsn3_1572 crossref_primary_10_1016_j_meatsci_2016_04_021 crossref_primary_10_3390_biology11020244 crossref_primary_10_1186_s40643_022_00529_z crossref_primary_10_1007_s12517_022_11100_7 crossref_primary_10_1007_s12649_015_9464_2 crossref_primary_10_1016_j_foodchem_2020_127369 crossref_primary_10_1111_jwas_12973 crossref_primary_10_1111_anu_13176 crossref_primary_10_3390_molecules25030494 crossref_primary_10_3390_polym15122658 crossref_primary_10_1016_j_heliyon_2024_e39655 crossref_primary_10_1016_j_lwt_2023_115515 crossref_primary_10_1016_j_aquaculture_2017_04_024 crossref_primary_10_4236_ajac_2021_125013 crossref_primary_10_1590_1678_4324_2019180621 crossref_primary_10_1016_j_ijbiomac_2024_132833 crossref_primary_10_1093_jas_skae057 crossref_primary_10_4236_fns_2016_714125 crossref_primary_10_3390_en14061768 crossref_primary_10_1186_s40643_016_0091_y crossref_primary_10_3390_ma13214964 crossref_primary_10_1016_j_foodhyd_2018_06_033 crossref_primary_10_1016_j_tifs_2021_05_002 crossref_primary_10_1080_00071668_2017_1293229 crossref_primary_10_1080_09506608_2020_1750807 crossref_primary_10_3390_su13168691 crossref_primary_10_1007_s12649_019_00693_y crossref_primary_10_52547_rap_12_34_78 crossref_primary_10_1186_s13765_020_00525_x crossref_primary_10_1080_03067319_2021_1910680 crossref_primary_10_1016_j_nbt_2018_09_003 crossref_primary_10_1007_s10123_018_0022_1 crossref_primary_10_1039_D3FB00041A crossref_primary_10_1016_j_bcab_2024_103407 crossref_primary_10_1016_j_procbio_2018_09_002 crossref_primary_10_6000_1929_5634_2014_03_02_6 crossref_primary_10_1111_ijfs_13636 crossref_primary_10_3390_fermentation8070317 crossref_primary_10_1007_s12649_016_9603_4 crossref_primary_10_1016_j_psj_2024_104596 crossref_primary_10_1016_j_matpr_2020_12_455 crossref_primary_10_1016_j_wasman_2019_10_026 crossref_primary_10_1039_C7FO01387F crossref_primary_10_1007_s12649_018_0424_5 crossref_primary_10_1016_j_jclepro_2019_119845 crossref_primary_10_1002_vnl_21861 crossref_primary_10_1021_acs_jafc_4c00827 |
Cites_doi | 10.1016/S0924-2244(01)00007-3 10.1016/S0141-0229(02)00024-8 10.1016/0960-8524(95)00009-4 10.1007/978-1-4757-4242-8_5 10.1177/0734242X10370378 10.1590/S1517-83822004000100015 10.1007/s11947-010-0357-x 10.1111/j.1745-4514.2011.00562.x 10.1007/s13197-010-0051-z 10.1111/j.1750-3841.2011.02057.x 10.1007/BF02731888 10.1186/1756-3305-3-3 10.1016/j.egypro.2011.05.063 10.1002/jsfa.2740650305 10.1016/S1381-1177(02)00203-5 10.1016/j.foodchem.2006.07.016 10.1016/j.peptides.2004.12.008 10.1080/08905430903102828 10.1007/s11745-001-0798-1 10.1007/s10068-011-0043-4 10.3382/ps.2008-00558 10.1016/j.biortech.2007.08.024 10.1016/j.wasman.2011.11.017 10.1016/j.compscitech.2004.09.030 10.1006/bbrc.1997.7698 10.1016/S0960-8524(01)00199-7 10.1016/j.biombioe.2011.01.034 10.1016/j.foodchem.2004.10.030 10.1016/j.cattod.2011.02.005 10.1016/j.biortech.2010.09.121 10.1016/j.resconrec.2011.04.004 10.11606/S1413-95962008000700008 10.1007/s11947-008-0091-9 10.1590/S1517-83822010000100028 10.1016/j.wasman.2011.09.004 10.3923/joafsnu.2009.84.89 10.1007/s11274-004-1556-2 10.1016/j.foodchem.2008.06.029 10.1016/j.biortech.2006.12.030 10.1016/j.jfoodeng.2004.10.011 10.1016/j.foodchem.2009.05.021 10.1111/j.1365-2621.2003.tb05746.x 10.1016/j.jaap.2010.04.005 10.1016/j.jfoodeng.2008.02.025 10.1111/j.1740-0929.2007.00507.x 10.1016/j.foodchem.2009.05.089 10.1016/j.biortech.2010.11.044 10.1016/j.foodchem.2008.10.050 10.1016/j.biortech.2005.05.021 10.1080/10408690091189266 10.1109/ICBBE.2010.5517934 10.1271/bbb.59.2239 10.1002/cjce.5450790110 10.1093/jaoac/93.5.1515 10.1016/j.radphyschem.2007.07.004 10.1016/j.biortech.2008.01.023 10.1016/j.supflu.2005.03.001 10.1016/S0960-8524(99)90072-X 10.1016/j.biortech.2008.09.047 10.3390/md7040803 10.1016/j.jbiosc.2008.10.018 10.1016/j.biortech.2006.10.034 10.1007/s13197-010-0137-7 10.2306/scienceasia1513-1874.2010.36.137 10.1016/j.jhazmat.2008.03.109 10.1016/j.procbio.2011.05.023 10.1046/j.1365-2672.2000.01173.x 10.1016/j.foodres.2009.02.014 10.1016/j.biortech.2004.10.014 10.2225/vol8-issue1-fulltext-6 10.1016/S0308-8146(97)00199-4 10.1007/s11746-010-1689-4 10.1016/j.procbio.2010.02.020 10.1016/0269-7483(89)90092-X 10.1021/bp9900920 10.1016/j.renene.2007.05.001 10.1016/j.biortech.2007.09.006 10.1017/S0022029999003982 10.1016/S0196-8904(03)00177-8 10.1016/j.wasman.2011.03.024 10.1139/w04-123 10.1021/bk-1997-0674.ch008 10.1016/S0269-7491(98)80105-X 10.1016/S0377-8401(96)01109-1 10.1016/j.foodhyd.2011.02.007 10.1016/j.pep.2005.02.015 10.1111/j.1365-2672.1989.tb04951.x 10.1016/S0960-8524(97)00182-X 10.1631/jzus.B061620 10.1039/B507441J 10.1038/sj.jim.2900706 10.1016/j.foodchem.2009.12.027 10.1016/j.foodchem.2009.10.055 10.1016/j.compositesb.2009.04.011 10.1021/jf970294g 10.1016/j.foodres.2005.10.010 10.2298/BAH0902143O 10.1016/S0960-8524(97)00081-3 10.1016/S0734-9750(99)00027-0 10.1016/j.cej.2005.03.006 10.1111/j.1740-0929.2008.00601.x 10.1016/j.procbio.2007.10.007 10.1002/jsfa.1092 10.1111/j.1365-2621.2004.tb09909.x 10.1016/j.biotechadv.2005.11.004 10.1007/BF01028496 10.1007/s10532-009-9256-0 10.1016/j.foodchem.2008.05.049 10.1070/RC2005v074n01ABEH001167 10.1016/S0963-9969(03)00104-2 10.1016/S0032-9592(02)00251-0 10.1007/s00253-005-0239-8 10.1016/j.foodchem.2005.12.019 10.1016/S0308-8146(00)00052-2 10.1007/s00253-009-2398-5 10.1016/j.jff.2011.09.001 10.1016/S0924-2244(02)00021-3 10.1016/j.micres.2006.07.013 10.1093/ps/76.3.491 10.1155/2011/837875 10.1016/j.bej.2010.12.004 10.1093/ps/80.1.79 10.1016/j.procbio.2004.06.033 10.1111/j.1365-2621.1997.tb03987.x 10.1021/jf970649w 10.1016/j.rser.2011.09.015 10.1021/jf072669w 10.3382/ps.0700085 10.1016/S0032-9592(00)00176-X 10.1111/j.1740-0929.2008.00584.x 10.1128/AEM.63.2.790-792.1997 10.1016/j.wasman.2010.12.005 10.1016/j.progpolymsci.2012.04.003 10.3382/ps.0710765 10.1007/s11274-007-9398-3 10.1111/j.1750-3841.2007.00610.x 10.1007/s00284-006-0308-y 10.1007/s11947-010-0416-3 10.1007/s00253-002-0975-y 10.1128/AEM.61.4.1469-1474.1995 10.1016/j.compscitech.2004.06.011 10.1007/s11746-003-0799-5 10.1016/j.foodchem.2010.09.039 10.1111/j.1541-4337.2009.00069.x 10.1016/j.fuel.2009.07.017 10.1016/j.biortech.2005.12.017 10.1002/mame.201000095 10.5483/BMBRep.2002.35.2.239 10.1111/j.1365-2672.2011.05103.x 10.1016/S0032-9592(01)00206-0 10.3136/fstr.9.91 10.1016/S0960-8524(03)00147-0 10.1016/S0309-1740(99)00125-4 |
ContentType | Journal Article |
Copyright | 2012 Elsevier Ltd Copyright © 2012 Elsevier Ltd. All rights reserved. |
Copyright_xml | – notice: 2012 Elsevier Ltd – notice: Copyright © 2012 Elsevier Ltd. All rights reserved. |
DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 7S9 L.6 OTOTI |
DOI | 10.1016/j.wasman.2012.08.001 |
DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic AGRICOLA AGRICOLA - Academic OSTI.GOV |
DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
DatabaseTitleList | MEDLINE - Academic AGRICOLA MEDLINE |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Engineering Chemistry |
EISSN | 1879-2456 |
EndPage | 565 |
ExternalDocumentID | 22439949 22985619 10_1016_j_wasman_2012_08_001 S0956053X12003674 |
Genre | Journal Article Review |
GroupedDBID | --- --K --M -~X .DC .~1 0R~ 123 1B1 1RT 1~. 1~5 29R 4.4 457 4G. 53G 5VS 7-5 71M 8P~ 9JM 9JN AABNK AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAQXK AAXUO ABEFU ABFNM ABFYP ABJNI ABLST ABMAC ABQEM ABQYD ABXDB ABYKQ ACDAQ ACGFS ACLVX ACRLP ACSBN ADBBV ADEZE ADMUD AEBSH AEKER AENEX AFKWA AFTJW AFXIZ AGHFR AGUBO AGYEJ AHEUO AHHHB AIEXJ AIKHN AITUG AJBFU AJOXV AKIFW ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ASPBG ATOGT AVWKF AXJTR AZFZN BKOJK BLECG BLXMC CS3 EBS EFJIC EFLBG EJD EO8 EO9 EP2 EP3 F5P FDB FEDTE FGOYB FIRID FNPLU FYGXN G-2 G-Q GBLVA HMC HVGLF HZ~ IHE IMUCA J1W KCYFY KOM LY9 M41 MO0 N9A O-L O9- OAUVE OZT P-8 P-9 P2P PC. Q38 R2- RIG ROL RPZ SDF SDG SEN SES SEW SPC SPCBC SSE SSJ SSZ T5K TAE WUQ Y6R ~02 ~G- AAHBH AATTM AAXKI AAYWO AAYXX ABWVN ACRPL ACVFH ADCNI ADNMO AEGFY AEIPS AEUPX AFJKZ AFPUW AGCQF AGQPQ AGRNS AIGII AIIUN AKBMS AKRWK AKYEP ANKPU APXCP BNPGV CITATION SSH CGR CUY CVF ECM EIF NPM 7X8 ACLOT EFKBS ~HD 7S9 L.6 AALMO AAPBV ABPIF ABPTK OTOTI |
ID | FETCH-LOGICAL-c489t-163ef99a2c96f241500cda5641f054638d2a31d5ebce13607a8e8e4b13dd47193 |
IEDL.DBID | AIKHN |
ISSN | 0956-053X 1879-2456 |
IngestDate | Thu May 18 18:28:52 EDT 2023 Sat Sep 27 23:40:41 EDT 2025 Sat Sep 27 21:29:25 EDT 2025 Thu Apr 03 06:59:53 EDT 2025 Thu Apr 24 22:58:38 EDT 2025 Tue Jul 01 02:59:24 EDT 2025 Fri Feb 23 02:24:44 EST 2024 |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 3 |
Keywords | Keratin Chicken by-products Bioresource Proteases Polyunsaturated fatty acids Protein hydrolysates |
Language | English |
License | https://www.elsevier.com/tdm/userlicense/1.0 Copyright © 2012 Elsevier Ltd. All rights reserved. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c489t-163ef99a2c96f241500cda5641f054638d2a31d5ebce13607a8e8e4b13dd47193 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23 |
PMID | 22985619 |
PQID | 1314708461 |
PQPubID | 23479 |
PageCount | 14 |
ParticipantIDs | osti_scitechconnect_22439949 proquest_miscellaneous_1710230687 proquest_miscellaneous_1314708461 pubmed_primary_22985619 crossref_citationtrail_10_1016_j_wasman_2012_08_001 crossref_primary_10_1016_j_wasman_2012_08_001 elsevier_sciencedirect_doi_10_1016_j_wasman_2012_08_001 |
ProviderPackageCode | CITATION AAYXX |
PublicationCentury | 2000 |
PublicationDate | 2013-03-01 |
PublicationDateYYYYMMDD | 2013-03-01 |
PublicationDate_xml | – month: 03 year: 2013 text: 2013-03-01 day: 01 |
PublicationDecade | 2010 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States |
PublicationTitle | Waste management (Elmsford) |
PublicationTitleAlternate | Waste Manag |
PublicationYear | 2013 |
Publisher | Elsevier Ltd |
Publisher_xml | – name: Elsevier Ltd |
References | Ouled Haddar, Zaghloul, Saeed (b0550) 2009; 20 Ramnani, Gupta (b0615) 2007; 23 Lin, Inglis, Yanke, Cheng (b0440) 1999; 23 Sereewatthanawut, Prapintip, Watchiraruji, Goto, Sasaki, Shotipruk (b0725) 2008; 99 Bougatef, Nedjar-Arroume, Manni, Ravallec, Barkia, Guillochon, Nasri (b0050) 2010; 118 Benjakul, Morrissey (b0030) 1997; 45 Chen, Muramoto, Yamauchi, Fujimoto, Nokihara (b0105) 1998; 46 Casarin, Cladera-Olivera, Brandelli (b0090) 2008; 1 Nchienzia, Morawicki, Gadang (b0520) 2010; 89 Zhang, G., Yue, X., Fan, A., Liu, G., 2010. Reutilization of waste chicken bone as nutrients source. In: Bioinformatics and Biomedical Engineering (iCBBE), 2010 4th International Conference, pp. 1–4. Raju, Rose, Muralidhara Rao (b0610) 1997; 66 Rutherfurd (b0660) 2010; 93 Huang, Ren, Jiang (b0305) 2011 Surówka, Fik (b0765) 1994; 65 Shareefdeen, Herner, Webb, Verhaeghe, Wilson (b0735) 2005; 113 Ockerman, Hansen (b0535) 2000 Rivera, Sebranek, Rust, Tabatabai (b0635) 2000; 55 Innis (b0320) 2004; 554 Clemente (b0140) 2001; 11 Gupta, Ramnani (b0265) 2006; 70 Palatsi, Viñas, Guivernau, Fernandez, Flotats (b0560) 2011; 102 Lin, Kelemen, Miller, Shih (b0445) 1995; 61 Lee, Jeon, Byun (b0425) 2011; 125 Gwyther, Williams, Golyshin, Edwards-Jones, Jones (b0270) 2011; 31 Najafi, Deobagkar, Deobagkar (b0500) 2005; 41 Tavakoli, Yoshida (b0785) 2006; 8 Galkin, Lunin (b0205) 2005; 74 Toldrá, Flores (b0790) 2000; 69 Corrêa, Peixoto, Gonçalves, Cabral (b0145) 2008; 88 Hwang, Shahidi, Onodenalore, Ho (b0310) 1997; 674 . Coward-Kelly, Chang, Agbogbo, Holtzapple (b0150) 2006; 97 Dalev (b0155) 1990; 12 European Union, Regulation (EC) No. 1096/2009 of the European Parliament and of the Council of 21 October 2009 Laying Down Health Rules as Regards Animal By-Products and Derived Products not Intended for Human Consumption and Repealing Regulation (EC) No. 1774/2002. Animal By-Products Regulation. Shaw, Brill, Clifford, Eckert, Ulrich Franck (b0740) 1991; 69 van Boekel (b0820) 2006; 24 Zhu, Zhu, Wan, Fan, Ma, Qian, Liu, Shen, Jiang (b0875) 2010; 88 Moritz, Latshaw (b0480) 2001; 80 Mane, Damle, Harikumar, Jamdar, Gade (b0450) 2010; 45 Sangtherapitiku, Chen, Chen (b0700) 2005; 3 Byun, Kim (b0075) 2002; 35 DudyDski, Kwiatkowski, Bajer (b0175) 2012; 32 Nascimento, Martins (b0510) 2004; 35 Sun, Hayakawa, Ogawa, Naknukool, Guan, Matsumoto (b0760) 2011; 20 Souissi, Ellouz-Triki, Bougatef, Blibech, Nasri (b0755) 2008; 163 USDA, 2011a. USDA International Egg and Poultry Review, vol. 14, August 2, pp. 1–3. ISSN: 1522–5100. Böckle, Müller (b0045) 1997; 63 Dey, Dora (b0170) 2011 Karamac, Flaczyk, Wanasundara, Amarowicz (b0360) 2005 Fakhfakh, Ktari, Haddar, Mnif, Dahmen, Nasri (b0195) 2011; 46 Guerard, Guimas, Binet (b0250) 2002; 19–20 Cheng, Lau, Liu, Zhao, Lam, Yin (b0115) 2009; 40 Kumar, Takagi (b0420) 1999; 17 Brandelli, Daroit, Riffel (b0055) 2010; 85 Khoddami, Ariffin, Bakar, Ghazali (b0380) 2009; 7 Voets, Kuppens, Cornelissen, Thewys (b0830) 2011; 35 Damle, Harikumar, Jamdar (b0160) 2010; 36 Wu, Chen, Shiau (b0850) 2003; 36 Gousterova, Nustorova, Paskaleva, Naydenov, Neshev, Vasileva-Tonkova (b0230) 2012; 6 Sant’Anna, Nascimento, Alexander, Dilger, Cavalcante, Diaz-Albiter, Bates, Dillon (b0705) 2010; 3 USDA, 2011b. Livestock and Poultry: World Market and Trade, April 2011. Gupta, Beg, Lorenz (b0260) 2002; 59 Kechaou, Dumay, Donnay-Moreno, Jaouen, Gouygou, Bergé, Amar (b0365) 2009; 107 Saiga, Iwai, Hayakawa, Takahata, Kitamura, Nishimura, Morimatsu (b0685) 2008; 56 Cascarosa, Gea, Arauzo (b0095) 2012; 16 Espósito, Amaral, Buarque, Oliveira, Carvalho, Bezerra (b0185) 2009; 112 Kang, Quitain, Daimon, Noda, Goto, Hu, Fujie (b0355) 2001; 79 Rossi, Flôres, Heck, Ayub (b0645) 2009; 23 Uddin, Ahn, Kishimura, Chun (b0800) 2010; 31 Bueno-Solano, López-Cervantes, Campas-Baypoli, Lauterio-García, Adan-Bante, Sánchez-Machado (b0065) 2009; 112 Giri, Sahoo, Sahu, Mukhopadhyay (b0235) 2000; 71 Hyun, Shin (b0315) 2000; 36 Okanovic, Ristic, Kormanjoš, Filipovic, Zˇivkovic (b0545) 2009; 25 Grazziotin, Pimentel, Sangali, de Jong, Brandelli (b0240) 2007; 98 Safari, Motamedzadegan, Ovissipour, Regenstein, Gildberg, Rasco (b0665) 2009; 0 Shahidi, Janak Kamil (b0730) 2001; 12 Jamdar, Harikumar (b0345) 2005; 96 Saha, Bandyopadhyaya, Dutta (b0670) 1990; 67 Kim, Mendis (b0395) 2006; 39 Kim, Lim, Suh (b0390) 2001; 37 Marculescu, Stan (b0460) 2011; 6 Grazziotin, Pimentel, Jong, Brandelli (b0245) 2008; 45 Cheng, Wan, Liu, Chen, Lin, Sakata (b0110) 2009; 80 Sahena, Zaidul, Jinap, Saari, Jahurul, Abbas, Norulaini (b0675) 2009; 8 Mante, Agblevor (b0455) 2012; 32 Rogalinski, Herrmann, Brunner (b0640) 2005; 36 Yoshida, Terashima, Takahashi (b0865) 1999; 15 Pihlanto-Leppälä, Koskinen, Phlola, Tupasela, Korhonen (b0600) 2000; 67 Uauy, Hoffman, Peirano, Birch, Birch (b0795) 2001; 36 Anwar, Saleemuddin (b0005) 1998; 64 Alvarez, Lidén (b0010) 2008; 33 Sarangi, Pattanaik, Rathinaraj, Sachindra, Madhusudan, Mahendrakar (b0710) 2011; 48 Wisniewski, Wiggers, Simionatto, Meier, Barros, Madureira (b0845) 2010; 89 Dunford, Temelli, LeBlanc (b0180) 1997; 62 Hsu, Lu, Jao (b0295) 2009; 42 Cheng, Zhu, Zhu, Qian, Zhu, Zhao, Chen (b0120) 2008; 99 Daoud, Dubois, Bors-Dodita, Nedjar-Arroume, Krier, Chihib, Mary, Kouach, Briand, Guillochon (b0165) 2005; 26 Jamdar, Rajalakshmi, Pednekar, Juan, Yardi, Sharma (b0330) 2010; 121 Zuta, Simpson, Chan, Phillips (b0880) 2003; 80 Patil, Nag (b0580) 2011; 88 Papadopoulos (b0570) 1989; 29 Muthukumar, Kandeepan (b0490) 2009; 1 Rathina Raj, Mahendrakar (b0625) 2010; 47 Plascencia-Jatomea, Olvera-Novoa, Arredondo-Figueroa, Hall, Shirai (b0605) 2002; 82 Resch, Wörl, Waltenberger, Braun, Kirchmayr (b0630) 2011; 102 Mazotto, Coelho, Cedrola, de Lima, Couri, Paraguai, Vermelho (b0470) 2011 Jamdar, Harikumar (b0335) 2008; 77 Pandey, Ahn, Lee, Mohanty, Misra (b0565) 2010; 295 Seo, Lee, Baek (b0720) 2008; 73 Cheng, Liu, Wan, Lin, Sakata (b0125) 2008; 79 Kurbanoglu, Kurbanoglu (b0415) 2002; 94 Salminen, Rintala (b0690) 2002; 83 Shinogi, Kanri (b0745) 2003; 90 Giménez, Alemán, Montero, Gómez-Guillén (b0220) 2009; 114 Bulushev, Ross (b0070) 2011; 171 Ghorbel, Souissi, Triki-Ellouz, Dufossé, Guérard, Nasri (b0215) 2005; 21 Gbogouri, Linder, Fanni, Parmentier (b0210) 2004; 69 Jamdar, Rajalakshmi, Sharma (b0325) 2012; 36 Liaset, Espe (b0430) 2008; 43 Wang, Parsons (b0835) 1997; 76 Pérez-Gálvez, Almécija, Espejo, Guadix, Guadix (b0585) 2011; 53 Periago, Vidal, Ros, Rincón, Martínez, López, Rodrigo, Martínez (b0590) 1998; 63 Sahena, Zaidul, Jinap, Yazid, Khatib, Norulaini (b0680) 2010; 120 Bhaskar, Modi, Govindaraju, Radha, Lalitha (b0035) 2007; 98 Ohba, Deguchi, Kishikawa, Arsyad, Mormura, Kida (b0540) 2003; 9 Syed, Lee, Li, Kim, Agasar (b0770) 2009; 100 Bhaskar, Mahendrakar (b0040) 2008; 99 Han, Damodaran (b0280) 1997; 240 Nilsang, Lertsiri, Suphantharika, Assavanig (b0530) 2005; 70 Barrena, Artola, Vázquez, Sánchez (b0015) 2009; 161 Barone, Schmidt, Liebner (b0025) 2005; 65 Yaman (b0855) 2004; 45 Cai, Pancorbo, Merka, Sander, Barnhart (b0085) 1995; 52 Choudhary, Jana, Jha (b0135) 2004; 11 Huang, Liu (b0300) 2010; 18 Cai, Lou, Zheng (b0080) 2008; B9 Gómez-Guillén, Giménez, López-Caballero, Montero (b0225) 2011; 25 Murado, González, Vázquez (b0485) 2009; 7 Guo, Tian, Small (b0255) 2010; 119 Harnedy, FitzGerald (b0285) 2012; 4 Márquez, Bracho, Archile, Rangel, Benítez (b0465) 2005; 93 Taskin, Kurbanoglu (b0780) 2011; 111 Yin, Wan, Pu, Bechtel, Sathivel (b0860) 2011; 76 Chang, Wu, Chiang (b0100) 2007; 100 Kristinsson, Rasco (b0410) 2000; 40 Šližyte, Daukšas, Falch, Storrø, Rustad (b0750) 2005; 40 Kalia, Dufresne, Cherian, Kaith, Avérous, Njuguna, Nassiopoulos (b0350) 2011; 2011 Nagal, Jain (b0495) 2010; 41 Rulkens, Klapwijk, Willers (b0650) 1998; 102 Korniłłowicz-Kowalska, Bohacz (b0405) 2011; 31 Mokrejs, Svoboda, Hrncirik, Janacova, Vasek (b0475) 2011; 29 Piazza, McAloon, Garcia (b0595) 2011; 55 Sathivel, Bechtel, Babbitt, Smiley, Crapo, Reppond, Prinyawiwatkul (b0715) 2003; 68 Williams, Lee, Garlich, Shih (b0840) 1991; 70 Cheng, Hu, Shen, Takagi, Asano, Tsai (b0130) 1995; 59 Tarté (b0775) 2009 Kherrati, Faid, Elyachioui, Wahmane (b0375) 1998; 63 Sangali, Brandelli (b0695) 2000; 89 Nazeer, Sampath Kumar, Naqash, Radhika, Kishore, Bhatt (b0515) 2009; 38 Brandelli, Riffel (b0060) 2005; 8 Barone, Schmidt (b0020) 2005; 65 Jamdar, Harikumar (b0340) 2008; 99 Ullah, Wu (b0805) 2012 Liaset, Julshamn, Espe (b0435) 2003; 38 Ramnani, Singh, Gupta (b0620) 2005; 51 Williams, Shih (b0885) 1989; 67 Park, Hyun (b0575) 2002; 30 Nakade, Kamishima, Inoue, Ahhmed, Kawahara, Nakayama, Maruyama, Numata, Ohta, Aoki, Muguruma (b0505) 2008; 79 Neklyudov, Ivankin, Berdutina (b0525) 2000; 36 Russell, Fletcher, Merka (b0655) 1992; 71 Vasileva-Tonkova, Nustorova, Gushterova (b0825) 2007; 54 Faruk, O., Bledzki, A.K., Fink, H., Sain, M., 2012. Biocomposites reinforced with natural fibers: 2000–2010. Prog. Polym. Sci. Haard (b0275) 1998; 52 Ovissipour, Abedian Kenari, Motamedzadegan, Nazari (b0555) 2012; 5 Klompong, Benjakul, Kantachote, Shahidi (b0400) 2007; 102 Innis (10.1016/j.wasman.2012.08.001_b0320) 2004; 554 Mante (10.1016/j.wasman.2012.08.001_b0455) 2012; 32 Mane (10.1016/j.wasman.2012.08.001_b0450) 2010; 45 Rathina Raj (10.1016/j.wasman.2012.08.001_b0625) 2010; 47 Corrêa (10.1016/j.wasman.2012.08.001_b0145) 2008; 88 Taskin (10.1016/j.wasman.2012.08.001_b0780) 2011; 111 Grazziotin (10.1016/j.wasman.2012.08.001_b0245) 2008; 45 Kechaou (10.1016/j.wasman.2012.08.001_b0365) 2009; 107 Rutherfurd (10.1016/j.wasman.2012.08.001_b0660) 2010; 93 Cai (10.1016/j.wasman.2012.08.001_b0085) 1995; 52 Shahidi (10.1016/j.wasman.2012.08.001_b0730) 2001; 12 Gómez-Guillén (10.1016/j.wasman.2012.08.001_b0225) 2011; 25 Jamdar (10.1016/j.wasman.2012.08.001_b0345) 2005; 96 Brandelli (10.1016/j.wasman.2012.08.001_b0055) 2010; 85 Sahena (10.1016/j.wasman.2012.08.001_b0675) 2009; 8 Najafi (10.1016/j.wasman.2012.08.001_b0500) 2005; 41 Rogalinski (10.1016/j.wasman.2012.08.001_b0640) 2005; 36 Kalia (10.1016/j.wasman.2012.08.001_b0350) 2011; 2011 Kumar (10.1016/j.wasman.2012.08.001_b0420) 1999; 17 Hsu (10.1016/j.wasman.2012.08.001_b0295) 2009; 42 Hyun (10.1016/j.wasman.2012.08.001_b0315) 2000; 36 Kurbanoglu (10.1016/j.wasman.2012.08.001_b0415) 2002; 94 Bougatef (10.1016/j.wasman.2012.08.001_b0050) 2010; 118 Syed (10.1016/j.wasman.2012.08.001_b0770) 2009; 100 Uddin (10.1016/j.wasman.2012.08.001_b0800) 2010; 31 Grazziotin (10.1016/j.wasman.2012.08.001_b0240) 2007; 98 Bhaskar (10.1016/j.wasman.2012.08.001_b0040) 2008; 99 Ouled Haddar (10.1016/j.wasman.2012.08.001_b0550) 2009; 20 Ramnani (10.1016/j.wasman.2012.08.001_b0620) 2005; 51 Ullah (10.1016/j.wasman.2012.08.001_b0805) 2012 Voets (10.1016/j.wasman.2012.08.001_b0830) 2011; 35 Han (10.1016/j.wasman.2012.08.001_b0280) 1997; 240 Patil (10.1016/j.wasman.2012.08.001_b0580) 2011; 88 10.1016/j.wasman.2012.08.001_b0815 Lin (10.1016/j.wasman.2012.08.001_b0440) 1999; 23 Periago (10.1016/j.wasman.2012.08.001_b0590) 1998; 63 Daoud (10.1016/j.wasman.2012.08.001_b0165) 2005; 26 Shareefdeen (10.1016/j.wasman.2012.08.001_b0735) 2005; 113 Wang (10.1016/j.wasman.2012.08.001_b0835) 1997; 76 Nazeer (10.1016/j.wasman.2012.08.001_b0515) 2009; 38 Ockerman (10.1016/j.wasman.2012.08.001_b0535) 2000 Rivera (10.1016/j.wasman.2012.08.001_b0635) 2000; 55 Benjakul (10.1016/j.wasman.2012.08.001_b0030) 1997; 45 Lin (10.1016/j.wasman.2012.08.001_b0445) 1995; 61 10.1016/j.wasman.2012.08.001_b0810 Muthukumar (10.1016/j.wasman.2012.08.001_b0490) 2009; 1 Saiga (10.1016/j.wasman.2012.08.001_b0685) 2008; 56 Galkin (10.1016/j.wasman.2012.08.001_b0205) 2005; 74 Bulushev (10.1016/j.wasman.2012.08.001_b0070) 2011; 171 Choudhary (10.1016/j.wasman.2012.08.001_b0135) 2004; 11 Murado (10.1016/j.wasman.2012.08.001_b0485) 2009; 7 Clemente (10.1016/j.wasman.2012.08.001_b0140) 2001; 11 Park (10.1016/j.wasman.2012.08.001_b0575) 2002; 30 Cai (10.1016/j.wasman.2012.08.001_b0080) 2008; B9 Toldrá (10.1016/j.wasman.2012.08.001_b0790) 2000; 69 Guo (10.1016/j.wasman.2012.08.001_b0255) 2010; 119 Byun (10.1016/j.wasman.2012.08.001_b0075) 2002; 35 Mokrejs (10.1016/j.wasman.2012.08.001_b0475) 2011; 29 Russell (10.1016/j.wasman.2012.08.001_b0655) 1992; 71 10.1016/j.wasman.2012.08.001_b0200 Marculescu (10.1016/j.wasman.2012.08.001_b0460) 2011; 6 Saha (10.1016/j.wasman.2012.08.001_b0670) 1990; 67 Liaset (10.1016/j.wasman.2012.08.001_b0435) 2003; 38 Williams (10.1016/j.wasman.2012.08.001_b0840) 1991; 70 Dunford (10.1016/j.wasman.2012.08.001_b0180) 1997; 62 Ramnani (10.1016/j.wasman.2012.08.001_b0615) 2007; 23 Salminen (10.1016/j.wasman.2012.08.001_b0690) 2002; 83 Resch (10.1016/j.wasman.2012.08.001_b0630) 2011; 102 Sathivel (10.1016/j.wasman.2012.08.001_b0715) 2003; 68 Mazotto (10.1016/j.wasman.2012.08.001_b0470) 2011 Ghorbel (10.1016/j.wasman.2012.08.001_b0215) 2005; 21 Lee (10.1016/j.wasman.2012.08.001_b0425) 2011; 125 Cheng (10.1016/j.wasman.2012.08.001_b0110) 2009; 80 Seo (10.1016/j.wasman.2012.08.001_b0720) 2008; 73 Harnedy (10.1016/j.wasman.2012.08.001_b0285) 2012; 4 Rulkens (10.1016/j.wasman.2012.08.001_b0650) 1998; 102 Huang (10.1016/j.wasman.2012.08.001_b0300) 2010; 18 Yoshida (10.1016/j.wasman.2012.08.001_b0865) 1999; 15 Safari (10.1016/j.wasman.2012.08.001_b0665) 2009; 0 Shinogi (10.1016/j.wasman.2012.08.001_b0745) 2003; 90 Cascarosa (10.1016/j.wasman.2012.08.001_b0095) 2012; 16 Kang (10.1016/j.wasman.2012.08.001_b0355) 2001; 79 Jamdar (10.1016/j.wasman.2012.08.001_b0330) 2010; 121 Chang (10.1016/j.wasman.2012.08.001_b0100) 2007; 100 Hwang (10.1016/j.wasman.2012.08.001_b0310) 1997; 674 Neklyudov (10.1016/j.wasman.2012.08.001_b0525) 2000; 36 Vasileva-Tonkova (10.1016/j.wasman.2012.08.001_b0825) 2007; 54 Sun (10.1016/j.wasman.2012.08.001_b0760) 2011; 20 Huang (10.1016/j.wasman.2012.08.001_b0305) 2011 Kim (10.1016/j.wasman.2012.08.001_b0390) 2001; 37 Yin (10.1016/j.wasman.2012.08.001_b0860) 2011; 76 Kim (10.1016/j.wasman.2012.08.001_b0395) 2006; 39 Okanovic (10.1016/j.wasman.2012.08.001_b0545) 2009; 25 Rossi (10.1016/j.wasman.2012.08.001_b0645) 2009; 23 Sangtherapitiku (10.1016/j.wasman.2012.08.001_b0700) 2005; 3 Shaw (10.1016/j.wasman.2012.08.001_b0740) 1991; 69 Guerard (10.1016/j.wasman.2012.08.001_b0250) 2002; 19–20 Souissi (10.1016/j.wasman.2012.08.001_b0755) 2008; 163 Zhu (10.1016/j.wasman.2012.08.001_b0875) 2010; 88 Gupta (10.1016/j.wasman.2012.08.001_b0260) 2002; 59 Cheng (10.1016/j.wasman.2012.08.001_b0130) 1995; 59 Damle (10.1016/j.wasman.2012.08.001_b0160) 2010; 36 Barrena (10.1016/j.wasman.2012.08.001_b0015) 2009; 161 10.1016/j.wasman.2012.08.001_b0190 Karamac (10.1016/j.wasman.2012.08.001_b0360) 2005 Sant’Anna (10.1016/j.wasman.2012.08.001_b0705) 2010; 3 Palatsi (10.1016/j.wasman.2012.08.001_b0560) 2011; 102 Jamdar (10.1016/j.wasman.2012.08.001_b0325) 2012; 36 Böckle (10.1016/j.wasman.2012.08.001_b0045) 1997; 63 Nilsang (10.1016/j.wasman.2012.08.001_b0530) 2005; 70 Anwar (10.1016/j.wasman.2012.08.001_b0005) 1998; 64 Papadopoulos (10.1016/j.wasman.2012.08.001_b0570) 1989; 29 Ohba (10.1016/j.wasman.2012.08.001_b0540) 2003; 9 Piazza (10.1016/j.wasman.2012.08.001_b0595) 2011; 55 Yaman (10.1016/j.wasman.2012.08.001_b0855) 2004; 45 Wu (10.1016/j.wasman.2012.08.001_b0850) 2003; 36 Márquez (10.1016/j.wasman.2012.08.001_b0465) 2005; 93 DudyDski (10.1016/j.wasman.2012.08.001_b0175) 2012; 32 Cheng (10.1016/j.wasman.2012.08.001_b0115) 2009; 40 Plascencia-Jatomea (10.1016/j.wasman.2012.08.001_b0605) 2002; 82 Dalev (10.1016/j.wasman.2012.08.001_b0155) 1990; 12 Tavakoli (10.1016/j.wasman.2012.08.001_b0785) 2006; 8 van Boekel (10.1016/j.wasman.2012.08.001_b0820) 2006; 24 Korniłłowicz-Kowalska (10.1016/j.wasman.2012.08.001_b0405) 2011; 31 Bueno-Solano (10.1016/j.wasman.2012.08.001_b0065) 2009; 112 Sahena (10.1016/j.wasman.2012.08.001_b0680) 2010; 120 Barone (10.1016/j.wasman.2012.08.001_b0025) 2005; 65 Espósito (10.1016/j.wasman.2012.08.001_b0185) 2009; 112 Klompong (10.1016/j.wasman.2012.08.001_b0400) 2007; 102 Pihlanto-Leppälä (10.1016/j.wasman.2012.08.001_b0600) 2000; 67 Kherrati (10.1016/j.wasman.2012.08.001_b0375) 1998; 63 Kristinsson (10.1016/j.wasman.2012.08.001_b0410) 2000; 40 Casarin (10.1016/j.wasman.2012.08.001_b0090) 2008; 1 Sereewatthanawut (10.1016/j.wasman.2012.08.001_b0725) 2008; 99 Surówka (10.1016/j.wasman.2012.08.001_b0765) 1994; 65 Šližyte (10.1016/j.wasman.2012.08.001_b0750) 2005; 40 Coward-Kelly (10.1016/j.wasman.2012.08.001_b0150) 2006; 97 Nascimento (10.1016/j.wasman.2012.08.001_b0510) 2004; 35 Ovissipour (10.1016/j.wasman.2012.08.001_b0555) 2012; 5 Fakhfakh (10.1016/j.wasman.2012.08.001_b0195) 2011; 46 Cheng (10.1016/j.wasman.2012.08.001_b0120) 2008; 99 Cheng (10.1016/j.wasman.2012.08.001_b0125) 2008; 79 Nagal (10.1016/j.wasman.2012.08.001_b0495) 2010; 41 Wisniewski (10.1016/j.wasman.2012.08.001_b0845) 2010; 89 Dey (10.1016/j.wasman.2012.08.001_b0170) 2011 Moritz (10.1016/j.wasman.2012.08.001_b0480) 2001; 80 Gupta (10.1016/j.wasman.2012.08.001_b0265) 2006; 70 Sangali (10.1016/j.wasman.2012.08.001_b0695) 2000; 89 Giri (10.1016/j.wasman.2012.08.001_b0235) 2000; 71 Gwyther (10.1016/j.wasman.2012.08.001_b0270) 2011; 31 Pandey (10.1016/j.wasman.2012.08.001_b0565) 2010; 295 Bhaskar (10.1016/j.wasman.2012.08.001_b0035) 2007; 98 Barone (10.1016/j.wasman.2012.08.001_b0020) 2005; 65 Gousterova (10.1016/j.wasman.2012.08.001_b0230) 2012; 6 10.1016/j.wasman.2012.08.001_b0870 Brandelli (10.1016/j.wasman.2012.08.001_b0060) 2005; 8 Gbogouri (10.1016/j.wasman.2012.08.001_b0210) 2004; 69 Giménez (10.1016/j.wasman.2012.08.001_b0220) 2009; 114 Jamdar (10.1016/j.wasman.2012.08.001_b0335) 2008; 77 Tarté (10.1016/j.wasman.2012.08.001_b0775) 2009 Nakade (10.1016/j.wasman.2012.08.001_b0505) 2008; 79 Uauy (10.1016/j.wasman.2012.08.001_b0795) 2001; 36 Jamdar (10.1016/j.wasman.2012.08.001_b0340) 2008; 99 Nchienzia (10.1016/j.wasman.2012.08.001_b0520) 2010; 89 Williams (10.1016/j.wasman.2012.08.001_b0885) 1989; 67 Khoddami (10.1016/j.wasman.2012.08.001_b0380) 2009; 7 Zuta (10.1016/j.wasman.2012.08.001_b0880) 2003; 80 Pérez-Gálvez (10.1016/j.wasman.2012.08.001_b0585) 2011; 53 Alvarez (10.1016/j.wasman.2012.08.001_b0010) 2008; 33 Raju (10.1016/j.wasman.2012.08.001_b0610) 1997; 66 Chen (10.1016/j.wasman.2012.08.001_b0105) 1998; 46 Liaset (10.1016/j.wasman.2012.08.001_b0430) 2008; 43 Sarangi (10.1016/j.wasman.2012.08.001_b0710) 2011; 48 Haard (10.1016/j.wasman.2012.08.001_b0275) 1998; 52 |
References_xml | – volume: 88 start-page: 381 year: 2008 end-page: 387 ident: b0145 article-title: Fractionation of fish oil with supercritical carbon dioxide publication-title: J. Food Eng. – volume: 5 start-page: 696 year: 2012 end-page: 705 ident: b0555 article-title: Optimization of enzymatic hydrolysis of visceral waste proteins of Yellowfin Tuna ( publication-title: Food Bioprocess Technol. – volume: 25 start-page: 1813 year: 2011 end-page: 1827 ident: b0225 article-title: Functional and bioactive properties of collagen and gelatin from alternative sources: a review publication-title: Food Hydrocoll. – volume: 66 start-page: 139 year: 1997 end-page: 147 ident: b0610 article-title: Enzymatic hydrolysis of tannery fleshings using chicken intestine proteases publication-title: Anim. Feed Sci. Technol. – volume: 295 start-page: 975 year: 2010 end-page: 989 ident: b0565 article-title: Recent advances in the application of natural fiber based composites publication-title: Macromol. Mater. Eng. – volume: 98 start-page: 388 year: 2007 end-page: 394 ident: b0035 article-title: Utilization of meat industry by products: protein hydrolysate from sheep visceral mass publication-title: Bioresour. Technol. – start-page: 133 year: 2005 end-page: 138 ident: b0360 article-title: Angiotensin I-converting enzyme (ACE) inhibitory activity of hydrolysates obtained from muscle food industry by-products – a short report publication-title: Pol. J. Food Nutr. Sci. – volume: 70 start-page: 85 year: 1991 end-page: 94 ident: b0840 article-title: Evaluation of a bacterial feather fermentation product, feather-lysate, as a feed protein publication-title: Poult. Sci. – volume: 80 start-page: 933 year: 2003 end-page: 936 ident: b0880 article-title: Concentrating PUFA from mackerel processing waste publication-title: JAOCS – J. Am. Oil. Chem. Soc. – volume: 40 start-page: 43 year: 2000 end-page: 81 ident: b0410 article-title: Fish protein hydrolysates: production, biochemical, and functional properties publication-title: Crit. Rev. Food Sci. Nutr. – volume: 43 start-page: 42 year: 2008 end-page: 48 ident: b0430 article-title: Nutritional composition of soluble and insoluble fractions obtained by enzymatic hydrolysis of fish-raw materials publication-title: Process Biochem. – volume: 97 start-page: 1337 year: 2006 end-page: 1343 ident: b0150 article-title: Lime treatment of keratinous materials for the generation of highly digestible animal feed: 1. Chicken feathers publication-title: Bioresour. Technol. – volume: 52 start-page: 69 year: 1995 end-page: 77 ident: b0085 article-title: Stabilization of poultry processing by-products and poultry carcasses through direct chemical acidification publication-title: Bioresour. Technol. – volume: 8 start-page: 59 year: 2009 end-page: 74 ident: b0675 article-title: PUFAs in fish: extraction, fractionation, importance in health publication-title: Compr. Rev. Food Sci. Food Saf. – volume: 55 start-page: 842 year: 2011 end-page: 848 ident: b0595 article-title: A renewable flocculant from a poultry slaughterhouse waste and preliminary estimate of production costs publication-title: Resour. Conserv. Recycl. – volume: 23 start-page: 229 year: 2009 end-page: 242 ident: b0645 article-title: Production of high-protein hydrolysate from poultry industry residue and their molecular profiles publication-title: Food Biotechnol. – volume: 73 start-page: 41 year: 2008 end-page: 46 ident: b0720 article-title: Evaluation of bitterness in enzymatic hydrolysates of soy protein isolate by taste dilution analysis publication-title: J. Food Sci. – volume: 69 start-page: 387 year: 2000 end-page: 395 ident: b0790 article-title: The use of muscle enzymes as predictors of pork meat quality publication-title: Food Chem. – volume: 59 start-page: 2239 year: 1995 end-page: 2243 ident: b0130 article-title: Production and characterization of keratinase of a feather-degrading publication-title: Biosci. Biotechnol. Biochem. – volume: 6 start-page: 467 year: 2012 end-page: 474 ident: b0230 article-title: Assessment of feather hydrolysate from thermophilic actinomycetes for soil amendment and biological control application publication-title: Int. J. Environ. Res. – start-page: 145 year: 2009 end-page: 171 ident: b0775 article-title: Meat-derived protein ingredients publication-title: Ingredients in Meat Products – volume: 89 start-page: 2273 year: 2010 end-page: 2280 ident: b0520 article-title: Enzymatic hydrolysis of poultry meal with endo- and exopeptidases publication-title: Poult. Sci. – volume: 67 start-page: 414 year: 1990 end-page: 416 ident: b0670 article-title: Lipid of hilsa fish ( publication-title: J. Ind. Chem. Soc. – volume: 8 start-page: 35 year: 2005 end-page: 42 ident: b0060 article-title: Production of an extracellular keratinase from publication-title: Electron. J. Biotechnol. – volume: 36 start-page: 49 year: 2005 end-page: 58 ident: b0640 article-title: Production of amino acids from bovine serum albumin by continuous sub-critical water hydrolysis publication-title: J. Supercrit. Fluids – volume: 30 start-page: 633 year: 2002 end-page: 638 ident: b0575 article-title: Antigenotoxic effects of the peptides derived from bovine blood plasma proteins publication-title: Enzyme Microb. Technol. – volume: 98 start-page: 3172 year: 2007 end-page: 3175 ident: b0240 article-title: Production of feather protein hydrolysate by keratinolytic bacterium. publication-title: Bioresour. Technol. – volume: 65 start-page: 683 year: 2005 end-page: 692 ident: b0025 article-title: Compounding and molding of polyethylene composites reinforced with keratin feather fiber publication-title: Compos. Sci. Technol. – volume: 119 start-page: 167 year: 2010 end-page: 172 ident: b0255 article-title: Generation of meat-like flavourings from enzymatic hydrolysates of proteins from publication-title: Food Chem. – volume: 24 start-page: 230 year: 2006 end-page: 233 ident: b0820 article-title: Formation of flavour compounds in the Maillard reaction publication-title: Biotechnol. Adv. – volume: 6 start-page: 550 year: 2011 end-page: 557 ident: b0460 article-title: Poultry processing industry waste to energy conversion publication-title: Energy Proc. – volume: 111 start-page: 826 year: 2011 end-page: 834 ident: b0780 article-title: Evaluation of waste chicken feathers as peptone source for bacterial growth publication-title: J. Appl. Microbiol. – volume: 36 start-page: 65 year: 2000 end-page: 71 ident: b0315 article-title: Utilization of bovine blood plasma proteins for the production of angiotensin I converting enzyme inhibitory peptides publication-title: Process Biochem. – volume: 118 start-page: 559 year: 2010 end-page: 565 ident: b0050 article-title: Purification and identification of novel antioxidant peptides from enzymatic hydrolysates of sardinelle ( publication-title: Food Chem. – volume: 83 start-page: 13 year: 2002 end-page: 26 ident: b0690 article-title: Anaerobic digestion of organic solid poultry slaughterhouse waste – a review publication-title: Bioresour. Technol. – reference: USDA, 2011a. USDA International Egg and Poultry Review, vol. 14, August 2, pp. 1–3. ISSN: 1522–5100. < – volume: 33 start-page: 726 year: 2008 end-page: 734 ident: b0010 article-title: Semi-continuous co-digestion of solid slaughterhouse waste, manure, and fruit and vegetable waste publication-title: Renew. Energy – volume: 36 start-page: 885 year: 2001 end-page: 895 ident: b0795 article-title: Essential fatty acids in visual and brain development publication-title: Lipids – volume: 99 start-page: 3337 year: 2008 end-page: 3341 ident: b0120 article-title: Hydrolysis technology of biomass waste to produce amino acids in sub-critical water publication-title: Bioresour. Technol. – volume: 90 start-page: 241 year: 2003 end-page: 247 ident: b0745 article-title: Pyrolysis of plant, animal and human waste: physical and chemical characterization of the pyrolytic products publication-title: Bioresour. Technol. – volume: 99 start-page: 4105 year: 2008 end-page: 4111 ident: b0040 article-title: Protein hydrolysate from visceral waste proteins of Catla ( publication-title: Bioresour. Technol. – volume: 113 start-page: 215 year: 2005 end-page: 220 ident: b0735 article-title: An odor predictive model for rendering applications publication-title: Chem. Eng. J. – volume: 79 start-page: 65 year: 2001 end-page: 70 ident: b0355 article-title: Optimization of amino acids production from waste fish entrails by hydrolysis in sub-and supercritical water publication-title: Can. J. Chem. Eng. – volume: 3 start-page: 3 year: 2010 ident: b0705 article-title: Chicken blood provides a suitable meal for the sand fly publication-title: Parasites Vectors – volume: 674 start-page: 76 year: 1997 end-page: 84 ident: b0310 article-title: Thermally generated flavors from seal protein hydrolysate publication-title: ACS Symp. Ser. – year: 2000 ident: b0535 article-title: Animal By-Product Processing and Utilization – volume: 23 start-page: 1537 year: 2007 end-page: 1540 ident: b0615 article-title: Keratinases vis-à-vis conventional proteases and feather degradation publication-title: World J. Microbiol. Biotechnol. – volume: 47 start-page: 320 year: 2010 end-page: 324 ident: b0625 article-title: Effect of ensiling and organic solvents treatment on proteolytic enzymes of layer chicken intestine publication-title: J. Food Sci. Technol. – volume: 102 start-page: 1317 year: 2007 end-page: 1327 ident: b0400 article-title: Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally ( publication-title: Food Chem. – reference: Zhang, G., Yue, X., Fan, A., Liu, G., 2010. Reutilization of waste chicken bone as nutrients source. In: Bioinformatics and Biomedical Engineering (iCBBE), 2010 4th International Conference, pp. 1–4. – volume: 85 start-page: 1735 year: 2010 end-page: 1750 ident: b0055 article-title: Biochemical features of microbial keratinases and their production and applications publication-title: Appl. Microbiol. Biotechnol. – volume: 100 start-page: 1868 year: 2009 end-page: 1871 ident: b0770 article-title: Production, characterization and application of keratinase from publication-title: Bioresour. Technol. – volume: 1 start-page: 301 year: 2008 end-page: 305 ident: b0090 article-title: Use of poultry byproduct for production of keratinolytic enzymes publication-title: Food Bioprocess Technol. – volume: 12 start-page: 71 year: 1990 end-page: 72 ident: b0155 article-title: An enzyme-alkaline hydrolysis of feather keratin for obtaining a protein concentrate for fodder publication-title: Biotechnol. Lett. – volume: 114 start-page: 976 year: 2009 end-page: 983 ident: b0220 article-title: Antioxidant and functional properties of gelatin hydrolysates obtained from skin of sole and squid publication-title: Food Chem. – volume: 240 start-page: 839 year: 1997 end-page: 843 ident: b0280 article-title: Stability of protease Q against autolysis and in sodium dodecyl sulfate and urea solutions publication-title: Biochem. Biophys. Res. Commun. – start-page: 1 year: 2011 end-page: 9 ident: b0170 article-title: Optimization of the production of shrimp waste protein hydrolysate using microbial proteases adopting response surface methodology publication-title: J. Food Sci. Technol – volume: 11 start-page: 659 year: 2004 end-page: 671 ident: b0135 article-title: Enzyme technology applications in leather processing publication-title: Ind. J. Chem. Technol. – volume: 55 start-page: 53 year: 2000 end-page: 59 ident: b0635 article-title: Composition and protein fractions of different meat by-products used for petfood compared with mechanically separated chicken (MSC) publication-title: Meat Sci. – volume: 11 start-page: 254 year: 2001 end-page: 262 ident: b0140 article-title: Enzymatic protein hydrolysates in human nutrition publication-title: Trends Food Sci. Technol. – volume: 35 start-page: 91 year: 2004 end-page: 96 ident: b0510 article-title: Production and properties of an extracellular protease from thermophilic publication-title: Braz. J. Microbiol. – volume: 94 start-page: 202 year: 2002 end-page: 206 ident: b0415 article-title: A new process for the utilization as peptone of ram horn waste publication-title: Soc. Biotechnol. Jpn. – volume: 40 start-page: 1415 year: 2005 end-page: 1424 ident: b0750 article-title: Yield and composition of different fractions obtained after enzymatic hydrolysis of cod () publication-title: Process Biochem. – volume: 3 start-page: 41 year: 2005 end-page: 45 ident: b0700 article-title: Utilization of spent hens as a flavouring base: 2. Flavoring products from spent hen meat hydrolysate publication-title: J. Food Technol. – volume: 29 start-page: 260 year: 2011 end-page: 267 ident: b0475 article-title: Processing poultry feathers into keratin hydrolysate through alkaline-enzymatic hydrolysis publication-title: Waste Manage. Res. – volume: 20 start-page: 687 year: 2009 end-page: 694 ident: b0550 article-title: Biodegradation of native feather keratin by publication-title: Biodegradation – volume: 12 start-page: 435 year: 2001 end-page: 464 ident: b0730 article-title: Enzymes from fish and aquatic invertebrates and their application in the food industry publication-title: Trends Food Sci. Technol. – volume: 39 start-page: 383 year: 2006 end-page: 393 ident: b0395 article-title: Bioactive compounds from marine processing byproducts – a review publication-title: Food Res. Int. – volume: 31 start-page: 1689 year: 2011 end-page: 1701 ident: b0405 article-title: Biodegradation of keratin waste: theory and practical aspects publication-title: Waste Manage. – volume: 36 start-page: 494 year: 2012 end-page: 501 ident: b0325 article-title: Antioxidant and ace inhibitory properties of poultry viscera protein hydrolysate and its peptide fractions publication-title: J. Food Biochem. – volume: 89 start-page: 735 year: 2000 end-page: 743 ident: b0695 article-title: Feather keratin hydrolysis by a publication-title: J. Appl. Microbiol. – volume: 62 start-page: 289 year: 1997 end-page: 294 ident: b0180 article-title: Supercritical CO publication-title: J. Food Sci. – volume: 125 start-page: 495 year: 2011 end-page: 499 ident: b0425 article-title: Effect of angiotensin I converting enzyme inhibitory peptide purified from skate skin hydrolysate publication-title: Food Chem. – volume: 120 start-page: 879 year: 2010 end-page: 885 ident: b0680 article-title: Fatty acid compositions of fish oil extracted from different parts of Indian mackerel ( publication-title: Food Chem. – volume: 96 start-page: 1276 year: 2005 end-page: 1284 ident: b0345 article-title: Autolytic degradation of chicken intestinal proteins publication-title: Bioresour. Technol. – volume: 23 start-page: 149 year: 1999 end-page: 153 ident: b0440 article-title: Selection and characterization of feather-degrading bacteria from canola meal compost publication-title: J. Ind. Microbiol. Biotechnol. – volume: 56 start-page: 9586 year: 2008 end-page: 9591 ident: b0685 article-title: Angiotensin I-converting enzyme-inhibitory peptides obtained from chicken collagen hydrolysate publication-title: J. Agric. Food Chem. – volume: 20 start-page: 303 year: 2011 end-page: 310 ident: b0760 article-title: Evaluation of angiotensin I-converting enzyme (ACE) inhibitory activities of hydrolysates generated from byproducts of freshwater clam publication-title: Food Sci. Biotechnol. – volume: 80 start-page: 79 year: 2001 end-page: 86 ident: b0480 article-title: Indicators of nutritional value of hydrolyzed feather meal publication-title: Poult. Sci. – volume: 52 start-page: 64 year: 1998 end-page: 67 ident: b0275 article-title: Specialty enzymes from marine organisms publication-title: Food Technol. – volume: 42 start-page: 647 year: 2009 end-page: 652 ident: b0295 article-title: Antioxidative properties of peptides prepared from tuna cooking juice hydrolysates with orientase ( publication-title: Food Res. Int. – volume: 53 start-page: 305 year: 2011 end-page: 310 ident: b0585 article-title: Bi-objective optimisation of the enzymatic hydrolysis of porcine blood protein publication-title: Biochem. Eng. J. – volume: 25 start-page: 143 year: 2009 end-page: 152 ident: b0545 article-title: Chemical characteristics of poultry slaughterhouse by-products publication-title: Biotechnol. Anim. Husbandry – volume: 70 start-page: 21 year: 2006 end-page: 33 ident: b0265 article-title: Microbial keratinases and their prospective applications: an overview publication-title: Appl. Microbiol. Biotechnol. – volume: 51 start-page: 191 year: 2005 end-page: 196 ident: b0620 article-title: Keratinolytic potential of publication-title: Can. J. Microbiol. – volume: 2011 start-page: 1 year: 2011 end-page: 35 ident: b0350 article-title: Cellulose-based bio- and nanocomposites: a review publication-title: Int. J. Polym. Sci. – volume: 45 start-page: 1011 year: 2010 end-page: 1016 ident: b0450 article-title: Purification and characterization of aminopeptidase N from chicken intestine with potential application in debittering publication-title: Process Biochem. – volume: 35 start-page: 239 year: 2002 end-page: 243 ident: b0075 article-title: Structure and activity of angiotensin I converting enzyme inhibitory peptides derived from Alaskan pollack skin publication-title: J. Biochem. Mol. Biol. – year: 2012 ident: b0805 article-title: Feather fiber-based thermoplastics: effects of different plasticizers on material properties publication-title: Macromol. Mater. Eng. – volume: 61 start-page: 1469 year: 1995 end-page: 1474 ident: b0445 article-title: Nucleotide sequence and expression of kerA, the gene encoding a keratinolytic protease of publication-title: Appl. Environ. Microbiol. – start-page: 1527 year: 2011 end-page: 1532 ident: b0305 article-title: Separation of iron-binding peptides from shrimp processing by-products hydrolysates publication-title: Food Bioprocess Technol. – volume: 46 start-page: 49 year: 1998 end-page: 53 ident: b0105 article-title: Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein publication-title: J. Agric. Food Chem. – volume: 102 start-page: 2503 year: 2011 end-page: 2510 ident: b0630 article-title: Enhancement options for the utilisation of nitrogen rich animal by-products in anaerobic digestion publication-title: Bioresour. Technol. – volume: 79 start-page: 122 year: 2008 end-page: 128 ident: b0125 article-title: The development of angiotensin I-converting enzyme inhibitor derived from chicken bone protein publication-title: Anim. Sci. J. – volume: 76 start-page: 491 year: 1997 end-page: 496 ident: b0835 article-title: Effect of processing systems on protein quality of feather meals and hog hair meals publication-title: Poult. Sci. – volume: 64 start-page: 175 year: 1998 end-page: 183 ident: b0005 article-title: Alkaline proteases: a review publication-title: Bioresour. Technol – volume: 0 start-page: 1 year: 2009 end-page: 7 ident: b0665 article-title: Use of hydrolysates from Yellowfin Tuna ( publication-title: Food Bioprocess Technol – volume: 45 start-page: 651 year: 2004 end-page: 671 ident: b0855 article-title: Pyrolysis of biomass to produce fuels and chemical feedstocks publication-title: Energy Convers. Manage. – volume: 17 start-page: 561 year: 1999 end-page: 594 ident: b0420 article-title: Microbial alkaline proteases: from a bioindustrial viewpoint publication-title: Biotechnol. Adv. – volume: 71 start-page: 765 year: 1992 end-page: 770 ident: b0655 article-title: Lactic acid fermentation of broiler processing waste: physical properties and chemical analyses publication-title: Poult. Sci. – volume: 163 start-page: 473 year: 2008 end-page: 480 ident: b0755 article-title: Preparation and use of media for protease-producing bacterial strains based on by-products from Cuttlefish ( publication-title: Microbiol. Res. – volume: 45 start-page: 3423 year: 1997 end-page: 3430 ident: b0030 article-title: Protein hydrolysates from pacific whiting solid wastes publication-title: J. Agric. Food Chem. – volume: 69 start-page: C615 year: 2004 end-page: C622 ident: b0210 article-title: Influence of hydrolysis degree on the functional properties of salmon by-products hydrolysates publication-title: J. Food Sci. – volume: 32 start-page: 685 year: 2012 end-page: 691 ident: b0175 article-title: From feathers to syngas – technologies and devices publication-title: Waste Manage. – volume: 7 start-page: 127 year: 2009 end-page: 131 ident: b0380 article-title: Fatty acid profile of the oil extracted from fish waste (head, intestine and liver) ( publication-title: W. Appl. Sci. J. – volume: 102 start-page: 727 year: 1998 end-page: 735 ident: b0650 article-title: Recovery of valuable nitrogen compounds from agricultural liquid wastes: potential possibilities, bottlenecks and future technological challenges publication-title: Environ. Pollut. – volume: 15 start-page: 1090 year: 1999 end-page: 1094 ident: b0865 article-title: Production of organic acids and amino acids from fish meat by sub-critical water hydrolysis publication-title: Biotechnol. Prog. – volume: 65 start-page: 173 year: 2005 end-page: 181 ident: b0020 article-title: Polyethylene reinforced with keratin fibers obtained from chicken feathers publication-title: Compos. Sci. Technol. – volume: 31 start-page: 675 year: 2010 end-page: 679 ident: b0800 article-title: Production of valued materials from squid viscera by subcritical water hydrolysis publication-title: J. Environ. Biol. – volume: 100 start-page: 1537 year: 2007 end-page: 1543 ident: b0100 article-title: Antioxidant properties and protein compositions of porcine haemoglobin hydrolysates publication-title: Food Chem. – volume: 76 start-page: 283 year: 2011 end-page: 290 ident: b0860 article-title: Functional properties of protein fractions of channel catfish () publication-title: J. Food Sci. – volume: 38 start-page: 1747 year: 2003 end-page: 1759 ident: b0435 article-title: Chemical composition and theoretical nutritional evaluation of the produced fractions from enzymic hydrolysis of salmon frames with Protamex publication-title: Process Biochem. – volume: 82 start-page: 753 year: 2002 end-page: 759 ident: b0605 article-title: Feasibility of fishmeal replacement by shrimp head silage protein hydrolysate in Nile tilapia ( publication-title: J. Sci. Food Agric. – volume: 77 start-page: 467 year: 2008 end-page: 472 ident: b0335 article-title: Radiation decontamination of poultry viscera publication-title: Radiat. Phys. Chem. – volume: 18 start-page: 458 year: 2010 end-page: 463 ident: b0300 article-title: Inhibition of angiotensin I – converting enzymes by enzymatic hydrolysates from chicken blood publication-title: J. Food Drug Anal. – volume: 68 start-page: 2196 year: 2003 end-page: 2200 ident: b0715 article-title: Biochemical and functional properties of herring ( publication-title: J. Food Sci. – volume: 36 start-page: 452 year: 2000 end-page: 459 ident: b0525 article-title: Properties and uses of protein hydrolysates (review) publication-title: Appl. Biochem. Microbiol. – volume: 46 start-page: 1731 year: 2011 end-page: 1737 ident: b0195 article-title: Total solubilisation of the chicken feathers by fermentation with a keratinolytic bacterium, publication-title: Process Biochem. – volume: 59 start-page: 15 year: 2002 end-page: 32 ident: b0260 article-title: Bacterial alkaline proteases: molecular approaches and industrial applications publication-title: Appl. Microbiol. Biotechnol. – reference: European Union, Regulation (EC) No. 1096/2009 of the European Parliament and of the Council of 21 October 2009 Laying Down Health Rules as Regards Animal By-Products and Derived Products not Intended for Human Consumption and Repealing Regulation (EC) No. 1774/2002. Animal By-Products Regulation. – volume: 1 start-page: 84 year: 2009 end-page: 89 ident: b0490 article-title: Supplementation of four protein percentage to the basal diet of catfish () ( publication-title: J. Aquacult. Feed Sci. Nutr. – volume: 161 start-page: 380 year: 2009 end-page: 386 ident: b0015 article-title: The use of composting for the treatment of animal by-products: experiments at lab scale publication-title: J. Hazard. Mater. – volume: 74 start-page: 21 year: 2005 end-page: 35 ident: b0205 article-title: Subcritical and supercritical water: a universal medium for chemical reactions publication-title: Russ. Chem. Rev. – volume: 102 start-page: 2219 year: 2011 end-page: 2227 ident: b0560 article-title: Anaerobic digestion of slaughterhouse waste: main process limitations and microbial community interactions publication-title: Bioresour. Technol. – volume: 67 start-page: 25 year: 1989 end-page: 35 ident: b0885 article-title: Enumeration of some microbial groups in poultry waste digesters and enrichment of a feather degrading culture publication-title: J. Appl. Bacterial. – volume: 70 start-page: 571 year: 2005 end-page: 578 ident: b0530 article-title: Optimization of enzymatic hydrolysis of fish soluble concentrate by commercial proteases publication-title: J. Food Eng. – volume: 45 start-page: 61 year: 2008 end-page: 67 ident: b0245 article-title: Poultry feather hydrolysate as a protein source for growing rats publication-title: Braz. J. Vet. Res. Anim. Sci. – volume: 9 start-page: 91 year: 2003 end-page: 93 ident: b0540 article-title: Physiological functions of enzymatic hydrolysates of collagen or keratin contained in livestock and fish waste publication-title: Food Sci. Technol. Res. – volume: 171 start-page: 1 year: 2011 end-page: 13 ident: b0070 article-title: Catalysis for conversion of biomass to fuels via pyrolysis and gasification: a review publication-title: Catal. Today – start-page: 523780 year: 2011 ident: b0470 article-title: Keratinase production by three publication-title: Enzyme Res. – volume: 112 start-page: 671 year: 2009 end-page: 675 ident: b0065 article-title: Chemical and biological characteristics of protein hydrolysates from fermented shrimp by-products publication-title: Food Chem. – volume: 31 start-page: 767 year: 2011 end-page: 778 ident: b0270 article-title: The environmental and biosecurity characteristics of livestock carcass disposal methods: a review publication-title: Waste Manage. – volume: 35 start-page: 1912 year: 2011 end-page: 1924 ident: b0830 article-title: Economics of electricity and heat production by gasification or flash pyrolysis of short rotation coppice in Flanders (Belgium) publication-title: Biomass Bioenergy – volume: 38 start-page: 461 year: 2009 end-page: 463 ident: b0515 article-title: Lipid profiles of Threadfin bream ( publication-title: Ind. J. Mar. Sci. – volume: 107 start-page: 158 year: 2009 end-page: 164 ident: b0365 article-title: Enzymatic hydrolysis of cuttlefish ( publication-title: J. Biosci. Bioeng. – volume: 79 start-page: 710 year: 2008 end-page: 715 ident: b0505 article-title: Identification of an antihypertensive peptide derived from chicken bone extract publication-title: Anim. Sci. J. – volume: 69 start-page: 26 year: 1991 end-page: 39 ident: b0740 article-title: Supercritical water a medium for chemistry publication-title: Chem. Eng. News – volume: 4 start-page: 6 year: 2012 end-page: 24 ident: b0285 article-title: Bioactive peptides from marine processing waste and shellfish: a review publication-title: J. Funct. Foods – volume: 67 start-page: 53 year: 2000 end-page: 64 ident: b0600 article-title: Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides publication-title: J. Diary Res. – volume: 36 start-page: 949 year: 2003 end-page: 957 ident: b0850 article-title: Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel ( publication-title: Food Res. Int. – volume: 121 start-page: 178 year: 2010 end-page: 184 ident: b0330 article-title: Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate publication-title: Food Chem. – volume: 63 start-page: 790 year: 1997 end-page: 792 ident: b0045 article-title: Reduction of disulfide bonds by publication-title: Appl. Environ. Microbiol. – volume: 54 start-page: 54 year: 2007 end-page: 57 ident: b0825 article-title: New protein hydrolysates from collagen wastes used as peptone for bacterial growth publication-title: Curr. Microbiol. – reference: Faruk, O., Bledzki, A.K., Fink, H., Sain, M., 2012. Biocomposites reinforced with natural fibers: 2000–2010. Prog. Polym. Sci. – volume: 65 start-page: 289 year: 1994 end-page: 296 ident: b0765 article-title: Studies on the recovery of proteinaceous substances from chicken heads: II. Application of pepsin to the production of protein hydrolysate publication-title: J. Sci. Food Agric. – volume: 16 start-page: 942 year: 2012 end-page: 957 ident: b0095 article-title: Thermochemical processing of meat and bone meal: a review publication-title: Renew. Sustain. Energy Rev. – volume: 89 start-page: 563 year: 2010 end-page: 568 ident: b0845 article-title: Biofuels from waste fish oil pyrolysis: chemical composition publication-title: Fuel – volume: 554 start-page: 27 year: 2004 end-page: 43 ident: b0320 article-title: Polyunsaturated fatty acids in human milk: an essential role in infant development publication-title: Adv. Exp. Med. Biol. – volume: 36 start-page: 137 year: 2010 end-page: 141 ident: b0160 article-title: Chicken intestine: a source of aminopeptidases publication-title: Science Asia – volume: 99 start-page: 6934 year: 2008 end-page: 6940 ident: b0340 article-title: A rapid autolytic method for the preparation of protein hydrolysate from poultry viscera publication-title: Bioresour. Technol. – volume: 8 start-page: 100 year: 2006 end-page: 106 ident: b0785 article-title: Conversion of scallop viscera wastes to valuable compounds using sub-critical water publication-title: Green Chem. – volume: 41 start-page: 349 year: 2005 end-page: 354 ident: b0500 article-title: Purification and characterization of an extracellular α-amylase from publication-title: Protein Expr. Purif. – volume: 41 start-page: 196 year: 2010 end-page: 200 ident: b0495 article-title: Feather degradation by strains of publication-title: Braz. J. Microbiol. – volume: B9 start-page: 60 year: 2008 end-page: 67 ident: b0080 article-title: Keratinase production and keratin degradation by a mutant strain of publication-title: J. Zhejiang Univ. Sci. – volume: 93 start-page: 503 year: 2005 end-page: 505 ident: b0465 article-title: Proteins, isoleucine, lysine and methionine content of bovine, porcine and poultry blood and their fractions publication-title: Food Chem. – reference: >. – volume: 80 start-page: 91 year: 2009 end-page: 97 ident: b0110 article-title: Determination of angiotensin-I converting enzyme inhibitory peptides in chicken leg bone protein hydrolysate with alcalase publication-title: Anim. Sci. J. – volume: 40 start-page: 650 year: 2009 end-page: 654 ident: b0115 article-title: Mechanical and thermal properties of chicken feather fiber/PLA green composites publication-title: Compos. B Eng. – volume: 63 start-page: 75 year: 1998 end-page: 79 ident: b0375 article-title: Process for recycling slaughterhouses wastes and by-products by fermentation publication-title: Bioresour. Technol. – volume: 29 start-page: 123 year: 1989 end-page: 138 ident: b0570 article-title: Effect of processing on high-protein feedstuffs: a review publication-title: Biol. Wastes – volume: 7 start-page: 803 year: 2009 end-page: 815 ident: b0485 article-title: Recovery of proteolytic and collagenolytic activities from viscera by-products of rayfish ( publication-title: Mar. Drugs – volume: 19–20 start-page: 489 year: 2002 end-page: 498 ident: b0250 article-title: Production of tuna waste hydrolysates by a commercial neutral protease preparation publication-title: J. Mol. Catal. B – volume: 63 start-page: 71 year: 1998 end-page: 78 ident: b0590 article-title: Influence of enzymatic treatment on the nutritional and functional properties of pea flour publication-title: Food Chem. – volume: 88 start-page: 187 year: 2010 end-page: 191 ident: b0875 article-title: Hydrolysis technology and kinetics of poultry waste to produce amino acids in subcritical water publication-title: J. Anal. Appl. Pyrol. – volume: 71 start-page: 97 year: 2000 end-page: 101 ident: b0235 article-title: Nutrient digestibility and intestinal enzyme activity of publication-title: Bioresour. Technol. – volume: 88 start-page: 589 year: 2011 end-page: 593 ident: b0580 article-title: Production of PUFA concentrates from poultry and fish processing waste publication-title: JAOCS – J. Am. Oil. Chem. Soc. – volume: 99 start-page: 555 year: 2008 end-page: 561 ident: b0725 article-title: Extraction of protein and amino acids from deoiled rice bran by subcritical water hydrolysis publication-title: Bioresour. Technol. – volume: 32 start-page: 67 year: 2012 end-page: 76 ident: b0455 article-title: Storage stability of biocrude oils from fast pyrolysis of poultry litter publication-title: Waste Manage. – volume: 93 start-page: 1515 year: 2010 end-page: 1522 ident: b0660 article-title: Methodology for determining degree of hydrolysis of proteins in hydrolysates: a review publication-title: J. AOAC Int. – volume: 48 start-page: 36 year: 2011 end-page: 44 ident: b0710 article-title: Purification of alkaline protease from chicken intestine by aqueous two phase system of polyethylene glycol and sodium citrate publication-title: J. Food Sci. Technol. – volume: 21 start-page: 33 year: 2005 end-page: 38 ident: b0215 article-title: Preparation and testing of publication-title: World J. Microbiol. Biotechnol. – reference: USDA, 2011b. Livestock and Poultry: World Market and Trade, April 2011. < – volume: 26 start-page: 713 year: 2005 end-page: 719 ident: b0165 article-title: New antibacterial peptide derived from bovine hemoglobin publication-title: Peptides – volume: 112 start-page: 125 year: 2009 end-page: 130 ident: b0185 article-title: Fish processing waste as source of alkaline proteases for laundry detergent publication-title: Food Chem. – volume: 37 start-page: 287 year: 2001 end-page: 291 ident: b0390 article-title: Feather-degrading publication-title: Process Biochem. – volume: 11 start-page: 254 year: 2001 ident: 10.1016/j.wasman.2012.08.001_b0140 article-title: Enzymatic protein hydrolysates in human nutrition publication-title: Trends Food Sci. Technol. doi: 10.1016/S0924-2244(01)00007-3 – volume: 30 start-page: 633 year: 2002 ident: 10.1016/j.wasman.2012.08.001_b0575 article-title: Antigenotoxic effects of the peptides derived from bovine blood plasma proteins publication-title: Enzyme Microb. Technol. doi: 10.1016/S0141-0229(02)00024-8 – volume: 52 start-page: 69 year: 1995 ident: 10.1016/j.wasman.2012.08.001_b0085 article-title: Stabilization of poultry processing by-products and poultry carcasses through direct chemical acidification publication-title: Bioresour. Technol. doi: 10.1016/0960-8524(95)00009-4 – volume: 554 start-page: 27 year: 2004 ident: 10.1016/j.wasman.2012.08.001_b0320 article-title: Polyunsaturated fatty acids in human milk: an essential role in infant development publication-title: Adv. Exp. Med. Biol. doi: 10.1007/978-1-4757-4242-8_5 – volume: 29 start-page: 260 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0475 article-title: Processing poultry feathers into keratin hydrolysate through alkaline-enzymatic hydrolysis publication-title: Waste Manage. Res. doi: 10.1177/0734242X10370378 – volume: 35 start-page: 91 year: 2004 ident: 10.1016/j.wasman.2012.08.001_b0510 article-title: Production and properties of an extracellular protease from thermophilic Bacillus sp publication-title: Braz. J. Microbiol. doi: 10.1590/S1517-83822004000100015 – volume: 5 start-page: 696 year: 2012 ident: 10.1016/j.wasman.2012.08.001_b0555 article-title: Optimization of enzymatic hydrolysis of visceral waste proteins of Yellowfin Tuna (Thunnus albacares) publication-title: Food Bioprocess Technol. doi: 10.1007/s11947-010-0357-x – volume: 36 start-page: 494 year: 2012 ident: 10.1016/j.wasman.2012.08.001_b0325 article-title: Antioxidant and ace inhibitory properties of poultry viscera protein hydrolysate and its peptide fractions publication-title: J. Food Biochem. doi: 10.1111/j.1745-4514.2011.00562.x – volume: 47 start-page: 320 year: 2010 ident: 10.1016/j.wasman.2012.08.001_b0625 article-title: Effect of ensiling and organic solvents treatment on proteolytic enzymes of layer chicken intestine publication-title: J. Food Sci. Technol. doi: 10.1007/s13197-010-0051-z – volume: 76 start-page: 283 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0860 article-title: Functional properties of protein fractions of channel catfish () Ictalurus punctatus and their effects in an emulsion system publication-title: J. Food Sci. doi: 10.1111/j.1750-3841.2011.02057.x – volume: 31 start-page: 675 year: 2010 ident: 10.1016/j.wasman.2012.08.001_b0800 article-title: Production of valued materials from squid viscera by subcritical water hydrolysis publication-title: J. Environ. Biol. – volume: 36 start-page: 452 year: 2000 ident: 10.1016/j.wasman.2012.08.001_b0525 article-title: Properties and uses of protein hydrolysates (review) publication-title: Appl. Biochem. Microbiol. doi: 10.1007/BF02731888 – volume: 3 start-page: 3 year: 2010 ident: 10.1016/j.wasman.2012.08.001_b0705 article-title: Chicken blood provides a suitable meal for the sand fly Lutzomyia longipalpis and does not inhibit Leishmania development in the gut publication-title: Parasites Vectors doi: 10.1186/1756-3305-3-3 – volume: 6 start-page: 550 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0460 article-title: Poultry processing industry waste to energy conversion publication-title: Energy Proc. doi: 10.1016/j.egypro.2011.05.063 – volume: 65 start-page: 289 year: 1994 ident: 10.1016/j.wasman.2012.08.001_b0765 article-title: Studies on the recovery of proteinaceous substances from chicken heads: II. Application of pepsin to the production of protein hydrolysate publication-title: J. Sci. Food Agric. doi: 10.1002/jsfa.2740650305 – volume: 19–20 start-page: 489 year: 2002 ident: 10.1016/j.wasman.2012.08.001_b0250 article-title: Production of tuna waste hydrolysates by a commercial neutral protease preparation publication-title: J. Mol. Catal. B doi: 10.1016/S1381-1177(02)00203-5 – volume: 102 start-page: 1317 year: 2007 ident: 10.1016/j.wasman.2012.08.001_b0400 article-title: Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type publication-title: Food Chem. doi: 10.1016/j.foodchem.2006.07.016 – volume: 18 start-page: 458 year: 2010 ident: 10.1016/j.wasman.2012.08.001_b0300 article-title: Inhibition of angiotensin I – converting enzymes by enzymatic hydrolysates from chicken blood publication-title: J. Food Drug Anal. – volume: 26 start-page: 713 year: 2005 ident: 10.1016/j.wasman.2012.08.001_b0165 article-title: New antibacterial peptide derived from bovine hemoglobin publication-title: Peptides doi: 10.1016/j.peptides.2004.12.008 – volume: 23 start-page: 229 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0645 article-title: Production of high-protein hydrolysate from poultry industry residue and their molecular profiles publication-title: Food Biotechnol. doi: 10.1080/08905430903102828 – volume: 36 start-page: 885 year: 2001 ident: 10.1016/j.wasman.2012.08.001_b0795 article-title: Essential fatty acids in visual and brain development publication-title: Lipids doi: 10.1007/s11745-001-0798-1 – volume: 20 start-page: 303 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0760 article-title: Evaluation of angiotensin I-converting enzyme (ACE) inhibitory activities of hydrolysates generated from byproducts of freshwater clam publication-title: Food Sci. Biotechnol. doi: 10.1007/s10068-011-0043-4 – volume: 89 start-page: 2273 year: 2010 ident: 10.1016/j.wasman.2012.08.001_b0520 article-title: Enzymatic hydrolysis of poultry meal with endo- and exopeptidases publication-title: Poult. Sci. doi: 10.3382/ps.2008-00558 – volume: 99 start-page: 3337 year: 2008 ident: 10.1016/j.wasman.2012.08.001_b0120 article-title: Hydrolysis technology of biomass waste to produce amino acids in sub-critical water publication-title: Bioresour. Technol. doi: 10.1016/j.biortech.2007.08.024 – volume: 32 start-page: 685 year: 2012 ident: 10.1016/j.wasman.2012.08.001_b0175 article-title: From feathers to syngas – technologies and devices publication-title: Waste Manage. doi: 10.1016/j.wasman.2011.11.017 – volume: 7 start-page: 127 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0380 article-title: Fatty acid profile of the oil extracted from fish waste (head, intestine and liver) (Sardinella lemuru) publication-title: W. Appl. Sci. J. – volume: 65 start-page: 683 year: 2005 ident: 10.1016/j.wasman.2012.08.001_b0025 article-title: Compounding and molding of polyethylene composites reinforced with keratin feather fiber publication-title: Compos. Sci. Technol. doi: 10.1016/j.compscitech.2004.09.030 – volume: 240 start-page: 839 year: 1997 ident: 10.1016/j.wasman.2012.08.001_b0280 article-title: Stability of protease Q against autolysis and in sodium dodecyl sulfate and urea solutions publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.1997.7698 – volume: 83 start-page: 13 year: 2002 ident: 10.1016/j.wasman.2012.08.001_b0690 article-title: Anaerobic digestion of organic solid poultry slaughterhouse waste – a review publication-title: Bioresour. Technol. doi: 10.1016/S0960-8524(01)00199-7 – volume: 35 start-page: 1912 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0830 article-title: Economics of electricity and heat production by gasification or flash pyrolysis of short rotation coppice in Flanders (Belgium) publication-title: Biomass Bioenergy doi: 10.1016/j.biombioe.2011.01.034 – volume: 93 start-page: 503 year: 2005 ident: 10.1016/j.wasman.2012.08.001_b0465 article-title: Proteins, isoleucine, lysine and methionine content of bovine, porcine and poultry blood and their fractions publication-title: Food Chem. doi: 10.1016/j.foodchem.2004.10.030 – volume: 69 start-page: 26 year: 1991 ident: 10.1016/j.wasman.2012.08.001_b0740 article-title: Supercritical water a medium for chemistry publication-title: Chem. Eng. News – volume: 171 start-page: 1 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0070 article-title: Catalysis for conversion of biomass to fuels via pyrolysis and gasification: a review publication-title: Catal. Today doi: 10.1016/j.cattod.2011.02.005 – volume: 102 start-page: 2219 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0560 article-title: Anaerobic digestion of slaughterhouse waste: main process limitations and microbial community interactions publication-title: Bioresour. Technol. doi: 10.1016/j.biortech.2010.09.121 – volume: 55 start-page: 842 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0595 article-title: A renewable flocculant from a poultry slaughterhouse waste and preliminary estimate of production costs publication-title: Resour. Conserv. Recycl. doi: 10.1016/j.resconrec.2011.04.004 – volume: 45 start-page: 61 year: 2008 ident: 10.1016/j.wasman.2012.08.001_b0245 article-title: Poultry feather hydrolysate as a protein source for growing rats publication-title: Braz. J. Vet. Res. Anim. Sci. doi: 10.11606/S1413-95962008000700008 – volume: 1 start-page: 301 year: 2008 ident: 10.1016/j.wasman.2012.08.001_b0090 article-title: Use of poultry byproduct for production of keratinolytic enzymes publication-title: Food Bioprocess Technol. doi: 10.1007/s11947-008-0091-9 – volume: 41 start-page: 196 year: 2010 ident: 10.1016/j.wasman.2012.08.001_b0495 article-title: Feather degradation by strains of Bacillus isolated from decomposing feathers publication-title: Braz. J. Microbiol. doi: 10.1590/S1517-83822010000100028 – volume: 32 start-page: 67 year: 2012 ident: 10.1016/j.wasman.2012.08.001_b0455 article-title: Storage stability of biocrude oils from fast pyrolysis of poultry litter publication-title: Waste Manage. doi: 10.1016/j.wasman.2011.09.004 – volume: 1 start-page: 84 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0490 article-title: Supplementation of four protein percentage to the basal diet of catfish () (Mystus cavasius) fingerlings: to analyses the optimum level of protein and body composition of fish publication-title: J. Aquacult. Feed Sci. Nutr. doi: 10.3923/joafsnu.2009.84.89 – volume: 21 start-page: 33 year: 2005 ident: 10.1016/j.wasman.2012.08.001_b0215 article-title: Preparation and testing of Sardinella protein hydrolysates as nitrogen source for extracellular lipase production by Rhizopus oryzae publication-title: World J. Microbiol. Biotechnol. doi: 10.1007/s11274-004-1556-2 – volume: 112 start-page: 671 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0065 article-title: Chemical and biological characteristics of protein hydrolysates from fermented shrimp by-products publication-title: Food Chem. doi: 10.1016/j.foodchem.2008.06.029 – volume: 99 start-page: 555 year: 2008 ident: 10.1016/j.wasman.2012.08.001_b0725 article-title: Extraction of protein and amino acids from deoiled rice bran by subcritical water hydrolysis publication-title: Bioresour. Technol. doi: 10.1016/j.biortech.2006.12.030 – volume: 70 start-page: 571 year: 2005 ident: 10.1016/j.wasman.2012.08.001_b0530 article-title: Optimization of enzymatic hydrolysis of fish soluble concentrate by commercial proteases publication-title: J. Food Eng. doi: 10.1016/j.jfoodeng.2004.10.011 – volume: 118 start-page: 559 year: 2010 ident: 10.1016/j.wasman.2012.08.001_b0050 article-title: Purification and identification of novel antioxidant peptides from enzymatic hydrolysates of sardinelle (Sardinella aurita) by-products proteins publication-title: Food Chem. doi: 10.1016/j.foodchem.2009.05.021 – volume: 68 start-page: 2196 year: 2003 ident: 10.1016/j.wasman.2012.08.001_b0715 article-title: Biochemical and functional properties of herring (Clupea harengus) byproduct hydrolysates publication-title: J. Food Sci. doi: 10.1111/j.1365-2621.2003.tb05746.x – volume: 88 start-page: 187 year: 2010 ident: 10.1016/j.wasman.2012.08.001_b0875 article-title: Hydrolysis technology and kinetics of poultry waste to produce amino acids in subcritical water publication-title: J. Anal. Appl. Pyrol. doi: 10.1016/j.jaap.2010.04.005 – volume: 88 start-page: 381 year: 2008 ident: 10.1016/j.wasman.2012.08.001_b0145 article-title: Fractionation of fish oil with supercritical carbon dioxide publication-title: J. Food Eng. doi: 10.1016/j.jfoodeng.2008.02.025 – volume: 79 start-page: 122 year: 2008 ident: 10.1016/j.wasman.2012.08.001_b0125 article-title: The development of angiotensin I-converting enzyme inhibitor derived from chicken bone protein publication-title: Anim. Sci. J. doi: 10.1111/j.1740-0929.2007.00507.x – volume: 119 start-page: 167 year: 2010 ident: 10.1016/j.wasman.2012.08.001_b0255 article-title: Generation of meat-like flavourings from enzymatic hydrolysates of proteins from Brassica sp publication-title: Food Chem. doi: 10.1016/j.foodchem.2009.05.089 – volume: 102 start-page: 2503 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0630 article-title: Enhancement options for the utilisation of nitrogen rich animal by-products in anaerobic digestion publication-title: Bioresour. Technol. doi: 10.1016/j.biortech.2010.11.044 – volume: 114 start-page: 976 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0220 article-title: Antioxidant and functional properties of gelatin hydrolysates obtained from skin of sole and squid publication-title: Food Chem. doi: 10.1016/j.foodchem.2008.10.050 – volume: 97 start-page: 1337 year: 2006 ident: 10.1016/j.wasman.2012.08.001_b0150 article-title: Lime treatment of keratinous materials for the generation of highly digestible animal feed: 1. Chicken feathers publication-title: Bioresour. Technol. doi: 10.1016/j.biortech.2005.05.021 – start-page: 133 year: 2005 ident: 10.1016/j.wasman.2012.08.001_b0360 article-title: Angiotensin I-converting enzyme (ACE) inhibitory activity of hydrolysates obtained from muscle food industry by-products – a short report publication-title: Pol. J. Food Nutr. Sci. – volume: 40 start-page: 43 year: 2000 ident: 10.1016/j.wasman.2012.08.001_b0410 article-title: Fish protein hydrolysates: production, biochemical, and functional properties publication-title: Crit. Rev. Food Sci. Nutr. doi: 10.1080/10408690091189266 – ident: 10.1016/j.wasman.2012.08.001_b0870 doi: 10.1109/ICBBE.2010.5517934 – volume: 59 start-page: 2239 year: 1995 ident: 10.1016/j.wasman.2012.08.001_b0130 article-title: Production and characterization of keratinase of a feather-degrading Bacillus licheniformis PWD-1 publication-title: Biosci. Biotechnol. Biochem. doi: 10.1271/bbb.59.2239 – volume: 79 start-page: 65 year: 2001 ident: 10.1016/j.wasman.2012.08.001_b0355 article-title: Optimization of amino acids production from waste fish entrails by hydrolysis in sub-and supercritical water publication-title: Can. J. Chem. Eng. doi: 10.1002/cjce.5450790110 – volume: 93 start-page: 1515 year: 2010 ident: 10.1016/j.wasman.2012.08.001_b0660 article-title: Methodology for determining degree of hydrolysis of proteins in hydrolysates: a review publication-title: J. AOAC Int. doi: 10.1093/jaoac/93.5.1515 – volume: 77 start-page: 467 year: 2008 ident: 10.1016/j.wasman.2012.08.001_b0335 article-title: Radiation decontamination of poultry viscera publication-title: Radiat. Phys. Chem. doi: 10.1016/j.radphyschem.2007.07.004 – volume: 99 start-page: 6934 year: 2008 ident: 10.1016/j.wasman.2012.08.001_b0340 article-title: A rapid autolytic method for the preparation of protein hydrolysate from poultry viscera publication-title: Bioresour. Technol. doi: 10.1016/j.biortech.2008.01.023 – year: 2000 ident: 10.1016/j.wasman.2012.08.001_b0535 – volume: 36 start-page: 49 year: 2005 ident: 10.1016/j.wasman.2012.08.001_b0640 article-title: Production of amino acids from bovine serum albumin by continuous sub-critical water hydrolysis publication-title: J. Supercrit. Fluids doi: 10.1016/j.supflu.2005.03.001 – volume: 71 start-page: 97 year: 2000 ident: 10.1016/j.wasman.2012.08.001_b0235 article-title: Nutrient digestibility and intestinal enzyme activity of Clarias batrachus (Linn.) juveniles fed on dried fish and chicken viscera incorporated diets publication-title: Bioresour. Technol. doi: 10.1016/S0960-8524(99)90072-X – volume: 100 start-page: 1868 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0770 article-title: Production, characterization and application of keratinase from Streptomyces gulbargensis publication-title: Bioresour. Technol. doi: 10.1016/j.biortech.2008.09.047 – volume: 7 start-page: 803 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0485 article-title: Recovery of proteolytic and collagenolytic activities from viscera by-products of rayfish (Raja clavata) publication-title: Mar. Drugs doi: 10.3390/md7040803 – volume: 107 start-page: 158 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0365 article-title: Enzymatic hydrolysis of cuttlefish (Sepia officinalis) and sardine (Sardina pilchardus) viscera using commercial proteases: effects on lipid distribution and amino acid composition publication-title: J. Biosci. Bioeng. doi: 10.1016/j.jbiosc.2008.10.018 – volume: 11 start-page: 659 year: 2004 ident: 10.1016/j.wasman.2012.08.001_b0135 article-title: Enzyme technology applications in leather processing publication-title: Ind. J. Chem. Technol. – volume: 98 start-page: 3172 year: 2007 ident: 10.1016/j.wasman.2012.08.001_b0240 article-title: Production of feather protein hydrolysate by keratinolytic bacterium. Vibrio sp. kr2 publication-title: Bioresour. Technol. doi: 10.1016/j.biortech.2006.10.034 – volume: 48 start-page: 36 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0710 article-title: Purification of alkaline protease from chicken intestine by aqueous two phase system of polyethylene glycol and sodium citrate publication-title: J. Food Sci. Technol. doi: 10.1007/s13197-010-0137-7 – volume: 36 start-page: 137 year: 2010 ident: 10.1016/j.wasman.2012.08.001_b0160 article-title: Chicken intestine: a source of aminopeptidases publication-title: Science Asia doi: 10.2306/scienceasia1513-1874.2010.36.137 – volume: 161 start-page: 380 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0015 article-title: The use of composting for the treatment of animal by-products: experiments at lab scale publication-title: J. Hazard. Mater. doi: 10.1016/j.jhazmat.2008.03.109 – volume: 46 start-page: 1731 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0195 article-title: Total solubilisation of the chicken feathers by fermentation with a keratinolytic bacterium, Bacillus pumilus A1, and the production of protein hydrolysate with high antioxidative activity publication-title: Process Biochem. doi: 10.1016/j.procbio.2011.05.023 – volume: 89 start-page: 735 year: 2000 ident: 10.1016/j.wasman.2012.08.001_b0695 article-title: Feather keratin hydrolysis by a Vibrio sp. Strain kr2 publication-title: J. Appl. Microbiol. doi: 10.1046/j.1365-2672.2000.01173.x – volume: 42 start-page: 647 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0295 article-title: Antioxidative properties of peptides prepared from tuna cooking juice hydrolysates with orientase (Bacillus subtilis) publication-title: Food Res. Int. doi: 10.1016/j.foodres.2009.02.014 – volume: 96 start-page: 1276 year: 2005 ident: 10.1016/j.wasman.2012.08.001_b0345 article-title: Autolytic degradation of chicken intestinal proteins publication-title: Bioresour. Technol. doi: 10.1016/j.biortech.2004.10.014 – volume: 8 start-page: 35 year: 2005 ident: 10.1016/j.wasman.2012.08.001_b0060 article-title: Production of an extracellular keratinase from Chryseobacterium sp. growing on raw feathers publication-title: Electron. J. Biotechnol. doi: 10.2225/vol8-issue1-fulltext-6 – start-page: 523780 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0470 article-title: Keratinase production by three Bacillus spp. using feather meal and whole feather as substrate in a submerged fermentation publication-title: Enzyme Res. – volume: 63 start-page: 71 year: 1998 ident: 10.1016/j.wasman.2012.08.001_b0590 article-title: Influence of enzymatic treatment on the nutritional and functional properties of pea flour publication-title: Food Chem. doi: 10.1016/S0308-8146(97)00199-4 – volume: 88 start-page: 589 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0580 article-title: Production of PUFA concentrates from poultry and fish processing waste publication-title: JAOCS – J. Am. Oil. Chem. Soc. doi: 10.1007/s11746-010-1689-4 – volume: 45 start-page: 1011 year: 2010 ident: 10.1016/j.wasman.2012.08.001_b0450 article-title: Purification and characterization of aminopeptidase N from chicken intestine with potential application in debittering publication-title: Process Biochem. doi: 10.1016/j.procbio.2010.02.020 – volume: 29 start-page: 123 year: 1989 ident: 10.1016/j.wasman.2012.08.001_b0570 article-title: Effect of processing on high-protein feedstuffs: a review publication-title: Biol. Wastes doi: 10.1016/0269-7483(89)90092-X – volume: 15 start-page: 1090 year: 1999 ident: 10.1016/j.wasman.2012.08.001_b0865 article-title: Production of organic acids and amino acids from fish meat by sub-critical water hydrolysis publication-title: Biotechnol. Prog. doi: 10.1021/bp9900920 – volume: 33 start-page: 726 year: 2008 ident: 10.1016/j.wasman.2012.08.001_b0010 article-title: Semi-continuous co-digestion of solid slaughterhouse waste, manure, and fruit and vegetable waste publication-title: Renew. Energy doi: 10.1016/j.renene.2007.05.001 – volume: 99 start-page: 4105 year: 2008 ident: 10.1016/j.wasman.2012.08.001_b0040 article-title: Protein hydrolysate from visceral waste proteins of Catla (Catla catla): optimization of hydrolysis conditions for a commercial neutral protease publication-title: Bioresour. Technol. doi: 10.1016/j.biortech.2007.09.006 – volume: 67 start-page: 53 year: 2000 ident: 10.1016/j.wasman.2012.08.001_b0600 article-title: Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides publication-title: J. Diary Res. doi: 10.1017/S0022029999003982 – volume: 45 start-page: 651 year: 2004 ident: 10.1016/j.wasman.2012.08.001_b0855 article-title: Pyrolysis of biomass to produce fuels and chemical feedstocks publication-title: Energy Convers. Manage. doi: 10.1016/S0196-8904(03)00177-8 – volume: 31 start-page: 1689 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0405 article-title: Biodegradation of keratin waste: theory and practical aspects publication-title: Waste Manage. doi: 10.1016/j.wasman.2011.03.024 – volume: 51 start-page: 191 year: 2005 ident: 10.1016/j.wasman.2012.08.001_b0620 article-title: Keratinolytic potential of Bacillus licheniformis RG1: structural and biochemical mechanism of featherdegradation publication-title: Can. J. Microbiol. doi: 10.1139/w04-123 – volume: 674 start-page: 76 year: 1997 ident: 10.1016/j.wasman.2012.08.001_b0310 article-title: Thermally generated flavors from seal protein hydrolysate publication-title: ACS Symp. Ser. doi: 10.1021/bk-1997-0674.ch008 – volume: 102 start-page: 727 year: 1998 ident: 10.1016/j.wasman.2012.08.001_b0650 article-title: Recovery of valuable nitrogen compounds from agricultural liquid wastes: potential possibilities, bottlenecks and future technological challenges publication-title: Environ. Pollut. doi: 10.1016/S0269-7491(98)80105-X – volume: 66 start-page: 139 year: 1997 ident: 10.1016/j.wasman.2012.08.001_b0610 article-title: Enzymatic hydrolysis of tannery fleshings using chicken intestine proteases publication-title: Anim. Feed Sci. Technol. doi: 10.1016/S0377-8401(96)01109-1 – volume: 25 start-page: 1813 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0225 article-title: Functional and bioactive properties of collagen and gelatin from alternative sources: a review publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2011.02.007 – year: 2012 ident: 10.1016/j.wasman.2012.08.001_b0805 article-title: Feather fiber-based thermoplastics: effects of different plasticizers on material properties publication-title: Macromol. Mater. Eng. – volume: 41 start-page: 349 year: 2005 ident: 10.1016/j.wasman.2012.08.001_b0500 article-title: Purification and characterization of an extracellular α-amylase from Bacillus subtilis AX20 publication-title: Protein Expr. Purif. doi: 10.1016/j.pep.2005.02.015 – volume: 67 start-page: 25 year: 1989 ident: 10.1016/j.wasman.2012.08.001_b0885 article-title: Enumeration of some microbial groups in poultry waste digesters and enrichment of a feather degrading culture publication-title: J. Appl. Bacterial. doi: 10.1111/j.1365-2672.1989.tb04951.x – volume: 64 start-page: 175 year: 1998 ident: 10.1016/j.wasman.2012.08.001_b0005 article-title: Alkaline proteases: a review publication-title: Bioresour. Technol doi: 10.1016/S0960-8524(97)00182-X – volume: B9 start-page: 60 year: 2008 ident: 10.1016/j.wasman.2012.08.001_b0080 article-title: Keratinase production and keratin degradation by a mutant strain of Bacillus subtilis publication-title: J. Zhejiang Univ. Sci. doi: 10.1631/jzus.B061620 – volume: 3 start-page: 41 year: 2005 ident: 10.1016/j.wasman.2012.08.001_b0700 article-title: Utilization of spent hens as a flavouring base: 2. Flavoring products from spent hen meat hydrolysate publication-title: J. Food Technol. – volume: 8 start-page: 100 year: 2006 ident: 10.1016/j.wasman.2012.08.001_b0785 article-title: Conversion of scallop viscera wastes to valuable compounds using sub-critical water publication-title: Green Chem. doi: 10.1039/B507441J – volume: 6 start-page: 467 year: 2012 ident: 10.1016/j.wasman.2012.08.001_b0230 article-title: Assessment of feather hydrolysate from thermophilic actinomycetes for soil amendment and biological control application publication-title: Int. J. Environ. Res. – volume: 23 start-page: 149 year: 1999 ident: 10.1016/j.wasman.2012.08.001_b0440 article-title: Selection and characterization of feather-degrading bacteria from canola meal compost publication-title: J. Ind. Microbiol. Biotechnol. doi: 10.1038/sj.jim.2900706 – ident: 10.1016/j.wasman.2012.08.001_b0190 – volume: 121 start-page: 178 year: 2010 ident: 10.1016/j.wasman.2012.08.001_b0330 article-title: Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate publication-title: Food Chem. doi: 10.1016/j.foodchem.2009.12.027 – volume: 120 start-page: 879 year: 2010 ident: 10.1016/j.wasman.2012.08.001_b0680 article-title: Fatty acid compositions of fish oil extracted from different parts of Indian mackerel (Rastrelliger kanagurta) using various techniques of supercritical CO2 extraction publication-title: Food Chem. doi: 10.1016/j.foodchem.2009.10.055 – volume: 40 start-page: 650 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0115 article-title: Mechanical and thermal properties of chicken feather fiber/PLA green composites publication-title: Compos. B Eng. doi: 10.1016/j.compositesb.2009.04.011 – volume: 45 start-page: 3423 year: 1997 ident: 10.1016/j.wasman.2012.08.001_b0030 article-title: Protein hydrolysates from pacific whiting solid wastes publication-title: J. Agric. Food Chem. doi: 10.1021/jf970294g – volume: 39 start-page: 383 year: 2006 ident: 10.1016/j.wasman.2012.08.001_b0395 article-title: Bioactive compounds from marine processing byproducts – a review publication-title: Food Res. Int. doi: 10.1016/j.foodres.2005.10.010 – volume: 25 start-page: 143 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0545 article-title: Chemical characteristics of poultry slaughterhouse by-products publication-title: Biotechnol. Anim. Husbandry doi: 10.2298/BAH0902143O – volume: 63 start-page: 75 year: 1998 ident: 10.1016/j.wasman.2012.08.001_b0375 article-title: Process for recycling slaughterhouses wastes and by-products by fermentation publication-title: Bioresour. Technol. doi: 10.1016/S0960-8524(97)00081-3 – volume: 17 start-page: 561 year: 1999 ident: 10.1016/j.wasman.2012.08.001_b0420 article-title: Microbial alkaline proteases: from a bioindustrial viewpoint publication-title: Biotechnol. Adv. doi: 10.1016/S0734-9750(99)00027-0 – volume: 113 start-page: 215 year: 2005 ident: 10.1016/j.wasman.2012.08.001_b0735 article-title: An odor predictive model for rendering applications publication-title: Chem. Eng. J. doi: 10.1016/j.cej.2005.03.006 – volume: 80 start-page: 91 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0110 article-title: Determination of angiotensin-I converting enzyme inhibitory peptides in chicken leg bone protein hydrolysate with alcalase publication-title: Anim. Sci. J. doi: 10.1111/j.1740-0929.2008.00601.x – volume: 43 start-page: 42 year: 2008 ident: 10.1016/j.wasman.2012.08.001_b0430 article-title: Nutritional composition of soluble and insoluble fractions obtained by enzymatic hydrolysis of fish-raw materials publication-title: Process Biochem. doi: 10.1016/j.procbio.2007.10.007 – volume: 82 start-page: 753 year: 2002 ident: 10.1016/j.wasman.2012.08.001_b0605 article-title: Feasibility of fishmeal replacement by shrimp head silage protein hydrolysate in Nile tilapia (Oreochromis niloticus L.) diets publication-title: J. Sci. Food Agric. doi: 10.1002/jsfa.1092 – volume: 69 start-page: C615 year: 2004 ident: 10.1016/j.wasman.2012.08.001_b0210 article-title: Influence of hydrolysis degree on the functional properties of salmon by-products hydrolysates publication-title: J. Food Sci. doi: 10.1111/j.1365-2621.2004.tb09909.x – volume: 24 start-page: 230 year: 2006 ident: 10.1016/j.wasman.2012.08.001_b0820 article-title: Formation of flavour compounds in the Maillard reaction publication-title: Biotechnol. Adv. doi: 10.1016/j.biotechadv.2005.11.004 – volume: 12 start-page: 71 year: 1990 ident: 10.1016/j.wasman.2012.08.001_b0155 article-title: An enzyme-alkaline hydrolysis of feather keratin for obtaining a protein concentrate for fodder publication-title: Biotechnol. Lett. doi: 10.1007/BF01028496 – volume: 20 start-page: 687 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0550 article-title: Biodegradation of native feather keratin by Bacillus subtilis recombinant strains publication-title: Biodegradation doi: 10.1007/s10532-009-9256-0 – volume: 112 start-page: 125 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0185 article-title: Fish processing waste as source of alkaline proteases for laundry detergent publication-title: Food Chem. doi: 10.1016/j.foodchem.2008.05.049 – volume: 74 start-page: 21 year: 2005 ident: 10.1016/j.wasman.2012.08.001_b0205 article-title: Subcritical and supercritical water: a universal medium for chemical reactions publication-title: Russ. Chem. Rev. doi: 10.1070/RC2005v074n01ABEH001167 – volume: 36 start-page: 949 year: 2003 ident: 10.1016/j.wasman.2012.08.001_b0850 article-title: Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus) publication-title: Food Res. Int. doi: 10.1016/S0963-9969(03)00104-2 – volume: 38 start-page: 1747 year: 2003 ident: 10.1016/j.wasman.2012.08.001_b0435 article-title: Chemical composition and theoretical nutritional evaluation of the produced fractions from enzymic hydrolysis of salmon frames with Protamex publication-title: Process Biochem. doi: 10.1016/S0032-9592(02)00251-0 – volume: 70 start-page: 21 year: 2006 ident: 10.1016/j.wasman.2012.08.001_b0265 article-title: Microbial keratinases and their prospective applications: an overview publication-title: Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-005-0239-8 – volume: 100 start-page: 1537 year: 2007 ident: 10.1016/j.wasman.2012.08.001_b0100 article-title: Antioxidant properties and protein compositions of porcine haemoglobin hydrolysates publication-title: Food Chem. doi: 10.1016/j.foodchem.2005.12.019 – volume: 69 start-page: 387 year: 2000 ident: 10.1016/j.wasman.2012.08.001_b0790 article-title: The use of muscle enzymes as predictors of pork meat quality publication-title: Food Chem. doi: 10.1016/S0308-8146(00)00052-2 – start-page: 1 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0170 article-title: Optimization of the production of shrimp waste protein hydrolysate using microbial proteases adopting response surface methodology publication-title: J. Food Sci. Technol – volume: 85 start-page: 1735 year: 2010 ident: 10.1016/j.wasman.2012.08.001_b0055 article-title: Biochemical features of microbial keratinases and their production and applications publication-title: Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-009-2398-5 – volume: 4 start-page: 6 year: 2012 ident: 10.1016/j.wasman.2012.08.001_b0285 article-title: Bioactive peptides from marine processing waste and shellfish: a review publication-title: J. Funct. Foods doi: 10.1016/j.jff.2011.09.001 – volume: 38 start-page: 461 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0515 article-title: Lipid profiles of Threadfin bream (Nemipterus japonicus) organs publication-title: Ind. J. Mar. Sci. – volume: 12 start-page: 435 year: 2001 ident: 10.1016/j.wasman.2012.08.001_b0730 article-title: Enzymes from fish and aquatic invertebrates and their application in the food industry publication-title: Trends Food Sci. Technol. doi: 10.1016/S0924-2244(02)00021-3 – ident: 10.1016/j.wasman.2012.08.001_b0810 – volume: 163 start-page: 473 year: 2008 ident: 10.1016/j.wasman.2012.08.001_b0755 article-title: Preparation and use of media for protease-producing bacterial strains based on by-products from Cuttlefish (Sepia officinalis) and wastewaters from marine-products processing factories publication-title: Microbiol. Res. doi: 10.1016/j.micres.2006.07.013 – volume: 76 start-page: 491 year: 1997 ident: 10.1016/j.wasman.2012.08.001_b0835 article-title: Effect of processing systems on protein quality of feather meals and hog hair meals publication-title: Poult. Sci. doi: 10.1093/ps/76.3.491 – volume: 2011 start-page: 1 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0350 article-title: Cellulose-based bio- and nanocomposites: a review publication-title: Int. J. Polym. Sci. doi: 10.1155/2011/837875 – volume: 53 start-page: 305 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0585 article-title: Bi-objective optimisation of the enzymatic hydrolysis of porcine blood protein publication-title: Biochem. Eng. J. doi: 10.1016/j.bej.2010.12.004 – volume: 80 start-page: 79 year: 2001 ident: 10.1016/j.wasman.2012.08.001_b0480 article-title: Indicators of nutritional value of hydrolyzed feather meal publication-title: Poult. Sci. doi: 10.1093/ps/80.1.79 – volume: 52 start-page: 64 year: 1998 ident: 10.1016/j.wasman.2012.08.001_b0275 article-title: Specialty enzymes from marine organisms publication-title: Food Technol. – volume: 40 start-page: 1415 year: 2005 ident: 10.1016/j.wasman.2012.08.001_b0750 article-title: Yield and composition of different fractions obtained after enzymatic hydrolysis of cod () Gadus morhua by-products publication-title: Process Biochem. doi: 10.1016/j.procbio.2004.06.033 – volume: 62 start-page: 289 year: 1997 ident: 10.1016/j.wasman.2012.08.001_b0180 article-title: Supercritical CO2 extraction of oil and residual proteins from Atlantic mackerel (Scomber scombrus) as affected by moisture content publication-title: J. Food Sci. doi: 10.1111/j.1365-2621.1997.tb03987.x – volume: 67 start-page: 414 year: 1990 ident: 10.1016/j.wasman.2012.08.001_b0670 article-title: Lipid of hilsa fish (Hilsa ilisa) publication-title: J. Ind. Chem. Soc. – volume: 46 start-page: 49 year: 1998 ident: 10.1016/j.wasman.2012.08.001_b0105 article-title: Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein publication-title: J. Agric. Food Chem. doi: 10.1021/jf970649w – volume: 16 start-page: 942 year: 2012 ident: 10.1016/j.wasman.2012.08.001_b0095 article-title: Thermochemical processing of meat and bone meal: a review publication-title: Renew. Sustain. Energy Rev. doi: 10.1016/j.rser.2011.09.015 – volume: 56 start-page: 9586 year: 2008 ident: 10.1016/j.wasman.2012.08.001_b0685 article-title: Angiotensin I-converting enzyme-inhibitory peptides obtained from chicken collagen hydrolysate publication-title: J. Agric. Food Chem. doi: 10.1021/jf072669w – volume: 70 start-page: 85 year: 1991 ident: 10.1016/j.wasman.2012.08.001_b0840 article-title: Evaluation of a bacterial feather fermentation product, feather-lysate, as a feed protein publication-title: Poult. Sci. doi: 10.3382/ps.0700085 – volume: 36 start-page: 65 year: 2000 ident: 10.1016/j.wasman.2012.08.001_b0315 article-title: Utilization of bovine blood plasma proteins for the production of angiotensin I converting enzyme inhibitory peptides publication-title: Process Biochem. doi: 10.1016/S0032-9592(00)00176-X – volume: 79 start-page: 710 year: 2008 ident: 10.1016/j.wasman.2012.08.001_b0505 article-title: Identification of an antihypertensive peptide derived from chicken bone extract publication-title: Anim. Sci. J. doi: 10.1111/j.1740-0929.2008.00584.x – volume: 63 start-page: 790 year: 1997 ident: 10.1016/j.wasman.2012.08.001_b0045 article-title: Reduction of disulfide bonds by Streptomyces pactum during growth on chicken feathers publication-title: Appl. Environ. Microbiol. doi: 10.1128/AEM.63.2.790-792.1997 – volume: 0 start-page: 1 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0665 article-title: Use of hydrolysates from Yellowfin Tuna (Thunnus albacares) heads as a complex nitrogen source for lactic acid bacteria publication-title: Food Bioprocess Technol – volume: 31 start-page: 767 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0270 article-title: The environmental and biosecurity characteristics of livestock carcass disposal methods: a review publication-title: Waste Manage. doi: 10.1016/j.wasman.2010.12.005 – ident: 10.1016/j.wasman.2012.08.001_b0200 doi: 10.1016/j.progpolymsci.2012.04.003 – volume: 71 start-page: 765 year: 1992 ident: 10.1016/j.wasman.2012.08.001_b0655 article-title: Lactic acid fermentation of broiler processing waste: physical properties and chemical analyses publication-title: Poult. Sci. doi: 10.3382/ps.0710765 – start-page: 145 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0775 article-title: Meat-derived protein ingredients – volume: 23 start-page: 1537 year: 2007 ident: 10.1016/j.wasman.2012.08.001_b0615 article-title: Keratinases vis-à-vis conventional proteases and feather degradation publication-title: World J. Microbiol. Biotechnol. doi: 10.1007/s11274-007-9398-3 – volume: 73 start-page: 41 year: 2008 ident: 10.1016/j.wasman.2012.08.001_b0720 article-title: Evaluation of bitterness in enzymatic hydrolysates of soy protein isolate by taste dilution analysis publication-title: J. Food Sci. doi: 10.1111/j.1750-3841.2007.00610.x – volume: 54 start-page: 54 year: 2007 ident: 10.1016/j.wasman.2012.08.001_b0825 article-title: New protein hydrolysates from collagen wastes used as peptone for bacterial growth publication-title: Curr. Microbiol. doi: 10.1007/s00284-006-0308-y – start-page: 1527 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0305 article-title: Separation of iron-binding peptides from shrimp processing by-products hydrolysates publication-title: Food Bioprocess Technol. doi: 10.1007/s11947-010-0416-3 – ident: 10.1016/j.wasman.2012.08.001_b0815 – volume: 59 start-page: 15 year: 2002 ident: 10.1016/j.wasman.2012.08.001_b0260 article-title: Bacterial alkaline proteases: molecular approaches and industrial applications publication-title: Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-002-0975-y – volume: 61 start-page: 1469 year: 1995 ident: 10.1016/j.wasman.2012.08.001_b0445 article-title: Nucleotide sequence and expression of kerA, the gene encoding a keratinolytic protease of Bacillus licheniformis PWD-1 publication-title: Appl. Environ. Microbiol. doi: 10.1128/AEM.61.4.1469-1474.1995 – volume: 65 start-page: 173 year: 2005 ident: 10.1016/j.wasman.2012.08.001_b0020 article-title: Polyethylene reinforced with keratin fibers obtained from chicken feathers publication-title: Compos. Sci. Technol. doi: 10.1016/j.compscitech.2004.06.011 – volume: 80 start-page: 933 year: 2003 ident: 10.1016/j.wasman.2012.08.001_b0880 article-title: Concentrating PUFA from mackerel processing waste publication-title: JAOCS – J. Am. Oil. Chem. Soc. doi: 10.1007/s11746-003-0799-5 – volume: 125 start-page: 495 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0425 article-title: Effect of angiotensin I converting enzyme inhibitory peptide purified from skate skin hydrolysate publication-title: Food Chem. doi: 10.1016/j.foodchem.2010.09.039 – volume: 8 start-page: 59 year: 2009 ident: 10.1016/j.wasman.2012.08.001_b0675 article-title: PUFAs in fish: extraction, fractionation, importance in health publication-title: Compr. Rev. Food Sci. Food Saf. doi: 10.1111/j.1541-4337.2009.00069.x – volume: 89 start-page: 563 year: 2010 ident: 10.1016/j.wasman.2012.08.001_b0845 article-title: Biofuels from waste fish oil pyrolysis: chemical composition publication-title: Fuel doi: 10.1016/j.fuel.2009.07.017 – volume: 98 start-page: 388 year: 2007 ident: 10.1016/j.wasman.2012.08.001_b0035 article-title: Utilization of meat industry by products: protein hydrolysate from sheep visceral mass publication-title: Bioresour. Technol. doi: 10.1016/j.biortech.2005.12.017 – volume: 295 start-page: 975 year: 2010 ident: 10.1016/j.wasman.2012.08.001_b0565 article-title: Recent advances in the application of natural fiber based composites publication-title: Macromol. Mater. Eng. doi: 10.1002/mame.201000095 – volume: 35 start-page: 239 year: 2002 ident: 10.1016/j.wasman.2012.08.001_b0075 article-title: Structure and activity of angiotensin I converting enzyme inhibitory peptides derived from Alaskan pollack skin publication-title: J. Biochem. Mol. Biol. doi: 10.5483/BMBRep.2002.35.2.239 – volume: 111 start-page: 826 year: 2011 ident: 10.1016/j.wasman.2012.08.001_b0780 article-title: Evaluation of waste chicken feathers as peptone source for bacterial growth publication-title: J. Appl. Microbiol. doi: 10.1111/j.1365-2672.2011.05103.x – volume: 37 start-page: 287 year: 2001 ident: 10.1016/j.wasman.2012.08.001_b0390 article-title: Feather-degrading Bacillus species from poultry waste publication-title: Process Biochem. doi: 10.1016/S0032-9592(01)00206-0 – volume: 9 start-page: 91 year: 2003 ident: 10.1016/j.wasman.2012.08.001_b0540 article-title: Physiological functions of enzymatic hydrolysates of collagen or keratin contained in livestock and fish waste publication-title: Food Sci. Technol. Res. doi: 10.3136/fstr.9.91 – volume: 90 start-page: 241 year: 2003 ident: 10.1016/j.wasman.2012.08.001_b0745 article-title: Pyrolysis of plant, animal and human waste: physical and chemical characterization of the pyrolytic products publication-title: Bioresour. Technol. doi: 10.1016/S0960-8524(03)00147-0 – volume: 94 start-page: 202 year: 2002 ident: 10.1016/j.wasman.2012.08.001_b0415 article-title: A new process for the utilization as peptone of ram horn waste publication-title: Soc. Biotechnol. Jpn. – volume: 55 start-page: 53 year: 2000 ident: 10.1016/j.wasman.2012.08.001_b0635 article-title: Composition and protein fractions of different meat by-products used for petfood compared with mechanically separated chicken (MSC) publication-title: Meat Sci. doi: 10.1016/S0309-1740(99)00125-4 |
SSID | ssj0014810 |
Score | 2.4939878 |
SecondaryResourceType | review_article |
Snippet | By-products from different animal sources are currently being utilised for beneficial purposes. Chicken processing plants all over the world generate large... |
SourceID | osti proquest pubmed crossref elsevier |
SourceType | Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
StartPage | 552 |
SubjectTerms | 60 APPLIED LIFE SCIENCES Animal Feed animal organs animal wastes Animals bioactive properties biological resources BIOLOGICAL WASTES Bioresource bones BY-PRODUCTS byproducts CARBOXYLIC ACIDS Chicken by-products CHICKENS CONVERSION Culture Media DOMESTIC ANIMALS ENZYMES Fatty Acids, Unsaturated - isolation & purification Feathers FERTILIZERS Food-Processing Industry - methods hydrolysates Industrial Waste KERATIN legs livestock feeds MANAGEMENT OF RADIOACTIVE WASTES, AND NON-RADIOACTIVE WASTES FROM NUCLEAR FACILITIES microbiological quality Peptide Hydrolases - isolation & purification PEPTONE peptones Peptones - isolation & purification pet foods Pets POLLUTION Polyunsaturated fatty acids Poultry Products Proteases Protein Hydrolysates protein sources proteinases SAFETY value-added products WASTE DISPOSAL waste management |
Title | Potential of chicken by-products as sources of useful biological resources |
URI | https://dx.doi.org/10.1016/j.wasman.2012.08.001 https://www.ncbi.nlm.nih.gov/pubmed/22985619 https://www.proquest.com/docview/1314708461 https://www.proquest.com/docview/1710230687 https://www.osti.gov/biblio/22439949 |
Volume | 33 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9NAEB61yYFyQNAHBEpkpF5NvPbG3j1GEVUookKCSrmt9im1DXYUJ0Jc-O3M-BHBoVTiau1I653ZmW92Z78BuLDB5IWzMpYOMx0E8HlsCtxXLNWYfLhgRNNj6fN1vrjhV8vp8gDm_VsYKqvsfH_r0xtv3X2ZdKs5Wd_eTr4ShR6a0JJRfVVe8EMYphjtxQCGs4-fFtf7ywQuGlKChnKPBPoXdE2Z1w9df9dEhEqHglRXyR6KUIMKN93DQLQJSJfP4VmHJKNZO9kXcODLY3gy7xu4HcPTP7gGT-DqS7WlyiAUqUJEHVDufRmZn_G65XytI11H7VF-TSN2tQ-7VdSSNJEmo0130l-fws3lh2_zRdw1UogtF3IbI-byQUqdWpkHCtlJYp2e5pyFhOjwhUt1xtzUG-tZlieFFl54bljmHAYvmZ3BoKxK_wqigA6AaOJsqh03Bdc20N1tyPGLwVRuBFm_eMp2LOPU7GKl-nKyO9UuuaIlV9QDM2EjiPdS65Zl45HxRa8X9Ze1KAwEj0iekxpJikhyLVUToRgCGURqNP13vXoVaosuT3Tpq12tWMZ4kSBaY_8YQ3ANczBRjOBlaxv730lTKRCrytf_PfU3cJQ2vTioAO4cBtvNzr9FRLQ1Yzh8_4uNO7v_DdeGCN4 |
linkProvider | Elsevier |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LS-RAEC7c8eB6ENfd1fG1WdhrmHTSk6SPMijja1hYhbk1_QRfyWBmEP-9VXkM60EFr6ELOl3VVV91V38F8Md4nWbWiFBYzHQQwKehznBfsVhh8mG9zuseS5eTdHzNz6bD6QqMurcwVFbZ-v7Gp9feuv0yaFdzMLu5GfwjCj00oSmj-qo0419glVNT6x6sHp2ejyfLywSe16QENeUeCXQv6OoyrydVPSgiQqVDQaqrZG9FqF6Jm-5tIFoHpJNN2GiRZHDUTPYbrLhiC9ZGXQO3LVj_j2vwO5z9LedUGYQipQ-oA8qdKwL9HM4aztcqUFXQHOVXNGJROb-4DxqSJtJk8Nie9Fc_4Prk-Go0DttGCqHhuZiHiLmcF0LFRqSeQnYUGauGKWc-Ijr83MYqYXbotHEsSaNM5S53XLPEWgxeIvkJvaIs3A4EHh0A0cSZWFmuM66Mp7tbn-IXjalcH5Ju8aRpWcap2cW97MrJbmWz5JKWXFIPzIj1IVxKzRqWjQ_GZ51e5CtrkRgIPpDcJzWSFJHkGqomQjEEMojUaPq_O_VK1BZdnqjClYtKsoTxLEK0xt4ZQ3ANc7A868N2YxvL34ljkSNWFbufnvovWBtfXV7Ii9PJ-R58jeu-HFQMtw-9-ePCHSA6muvD1vpfABO9CsQ |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Potential+of+chicken+by-products+as+sources+of+useful+biological+resources&rft.jtitle=Waste+management+%28Elmsford%29&rft.au=Lasekan%2C+Adeseye&rft.au=Abu+Bakar%2C+Fatimah&rft.au=Halal+Products+Research+Institute%2C+Universiti+Putra+Malaysia%2C+43400+UPM+Serdang%2C+Selangor&rft.au=Hashim%2C+Dzulkifly&rft.date=2013-03-01&rft.issn=0956-053X&rft.eissn=1879-2456&rft.volume=33&rft.issue=3&rft_id=info:doi/10.1016%2FJ.WASMAN.2012.08.001&rft.externalDocID=22439949 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0956-053X&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0956-053X&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0956-053X&client=summon |