Polymers as Encapsulating Agents and Delivery Vehicles of Enzymes

Enzymes are versatile biomolecules with broad applications. Since they are biological molecules, they can be easily destabilized when placed in adverse environmental conditions, such as variations in temperature, pH, or ionic strength. In this sense, the use of protective structures, as polymeric ca...

Full description

Saved in:
Bibliographic Details
Published inPolymers Vol. 13; no. 23; p. 4061
Main Authors da S. Pereira, Adejanildo, Souza, Camila P. L., Moraes, Lidiane, Fontes-Sant’Ana, Gizele C., Amaral, Priscilla F. F.
Format Journal Article
LanguageEnglish
Published Basel MDPI AG 23.11.2021
MDPI
Subjects
Online AccessGet full text
ISSN2073-4360
2073-4360
DOI10.3390/polym13234061

Cover

Abstract Enzymes are versatile biomolecules with broad applications. Since they are biological molecules, they can be easily destabilized when placed in adverse environmental conditions, such as variations in temperature, pH, or ionic strength. In this sense, the use of protective structures, as polymeric capsules, has been an excellent approach to maintain the catalytic stability of enzymes during their application. Thus, in this review, we report the use of polymeric materials as enzyme encapsulation agents, recent technological developments related to this subject, and characterization methodologies and possible applications of the formed bioactive structures. Our search detected that the most explored methods for enzyme encapsulation are ionotropic gelation, spray drying, freeze-drying, nanoprecipitation, and electrospinning. α-chymotrypsin, lysozyme, and β-galactosidase were the most used enzymes in encapsulations, with chitosan and sodium alginate being the main polymers. Furthermore, most studies reported high encapsulation efficiency, enzyme activity maintenance, and stability improvement at pH, temperature, and storage. Therefore, the information presented here shows a direction for the development of encapsulation systems capable of stabilizing different enzymes and obtaining better performance during application.
AbstractList Enzymes are versatile biomolecules with broad applications. Since they are biological molecules, they can be easily destabilized when placed in adverse environmental conditions, such as variations in temperature, pH, or ionic strength. In this sense, the use of protective structures, as polymeric capsules, has been an excellent approach to maintain the catalytic stability of enzymes during their application. Thus, in this review, we report the use of polymeric materials as enzyme encapsulation agents, recent technological developments related to this subject, and characterization methodologies and possible applications of the formed bioactive structures. Our search detected that the most explored methods for enzyme encapsulation are ionotropic gelation, spray drying, freeze-drying, nanoprecipitation, and electrospinning. α-chymotrypsin, lysozyme, and β-galactosidase were the most used enzymes in encapsulations, with chitosan and sodium alginate being the main polymers. Furthermore, most studies reported high encapsulation efficiency, enzyme activity maintenance, and stability improvement at pH, temperature, and storage. Therefore, the information presented here shows a direction for the development of encapsulation systems capable of stabilizing different enzymes and obtaining better performance during application.
Enzymes are versatile biomolecules with broad applications. Since they are biological molecules, they can be easily destabilized when placed in adverse environmental conditions, such as variations in temperature, pH, or ionic strength. In this sense, the use of protective structures, as polymeric capsules, has been an excellent approach to maintain the catalytic stability of enzymes during their application. Thus, in this review, we report the use of polymeric materials as enzyme encapsulation agents, recent technological developments related to this subject, and characterization methodologies and possible applications of the formed bioactive structures. Our search detected that the most explored methods for enzyme encapsulation are ionotropic gelation, spray drying, freeze-drying, nanoprecipitation, and electrospinning. α-chymotrypsin, lysozyme, and β-galactosidase were the most used enzymes in encapsulations, with chitosan and sodium alginate being the main polymers. Furthermore, most studies reported high encapsulation efficiency, enzyme activity maintenance, and stability improvement at pH, temperature, and storage. Therefore, the information presented here shows a direction for the development of encapsulation systems capable of stabilizing different enzymes and obtaining better performance during application.Enzymes are versatile biomolecules with broad applications. Since they are biological molecules, they can be easily destabilized when placed in adverse environmental conditions, such as variations in temperature, pH, or ionic strength. In this sense, the use of protective structures, as polymeric capsules, has been an excellent approach to maintain the catalytic stability of enzymes during their application. Thus, in this review, we report the use of polymeric materials as enzyme encapsulation agents, recent technological developments related to this subject, and characterization methodologies and possible applications of the formed bioactive structures. Our search detected that the most explored methods for enzyme encapsulation are ionotropic gelation, spray drying, freeze-drying, nanoprecipitation, and electrospinning. α-chymotrypsin, lysozyme, and β-galactosidase were the most used enzymes in encapsulations, with chitosan and sodium alginate being the main polymers. Furthermore, most studies reported high encapsulation efficiency, enzyme activity maintenance, and stability improvement at pH, temperature, and storage. Therefore, the information presented here shows a direction for the development of encapsulation systems capable of stabilizing different enzymes and obtaining better performance during application.
Author Souza, Camila P. L.
Moraes, Lidiane
Fontes-Sant’Ana, Gizele C.
da S. Pereira, Adejanildo
Amaral, Priscilla F. F.
AuthorAffiliation 2 Biochemical Processes Technology Department, Chemistry Institute, Universidade do Estado do Rio de Janeiro, Rio de Janeiro 20550-013, Brazil; gizele.santana@uerj.br
1 Escola de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-909, Brazil; adejanildosp@gmail.com (A.d.S.P.); camila_lins@hotmail.com.br (C.P.L.S.); lidiane@eq.ufrj.br (L.M.)
AuthorAffiliation_xml – name: 1 Escola de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-909, Brazil; adejanildosp@gmail.com (A.d.S.P.); camila_lins@hotmail.com.br (C.P.L.S.); lidiane@eq.ufrj.br (L.M.)
– name: 2 Biochemical Processes Technology Department, Chemistry Institute, Universidade do Estado do Rio de Janeiro, Rio de Janeiro 20550-013, Brazil; gizele.santana@uerj.br
Author_xml – sequence: 1
  givenname: Adejanildo
  orcidid: 0000-0002-8329-9241
  surname: da S. Pereira
  fullname: da S. Pereira, Adejanildo
– sequence: 2
  givenname: Camila P. L.
  orcidid: 0000-0001-9088-7431
  surname: Souza
  fullname: Souza, Camila P. L.
– sequence: 3
  givenname: Lidiane
  surname: Moraes
  fullname: Moraes, Lidiane
– sequence: 4
  givenname: Gizele C.
  surname: Fontes-Sant’Ana
  fullname: Fontes-Sant’Ana, Gizele C.
– sequence: 5
  givenname: Priscilla F. F.
  orcidid: 0000-0001-8951-8639
  surname: Amaral
  fullname: Amaral, Priscilla F. F.
BookMark eNqFkUtPxCAUhYnROD5m6b6JGzdVWiilG5OJ78REF-qWUHo7g2GgQqsZf72MY6JjYmQDge-ce-9hF21aZwGhgwwfE1Lhk86ZxTwjOaGYZRtoJ8clSSlhePPHeYTGITzjuGjBWFZuoxGhnJOCFTtocr-0AB8SGZILq2QXBiN7bafJZAq2j_e2Sc7B6Ffwi-QJZloZCIlrI_0elWEfbbXSBBh_7Xvo8fLi4ew6vb27ujmb3KaKVHmfxmpFVTcNQAGVUhg3uaRU5rxRrC3rDDesJZTl0HKV8Zy0UtUlrkteM4ASS7KHjle-g-3k4k0aIzqv59IvRIbFMg6xFkcUnK4E3VDPoVFxGi-_RU5qsf5i9UxM3avgrKgwxdHg6MvAu5cBQi_mOigwRlpwQxA5w7wgnJQ0ooe_0Gc3eBvz-KSy2F6xpNIVpbwLwUP77wTkF690Hz_HLfvV5g_VBzv8pWM
CitedBy_id crossref_primary_10_1016_j_colsurfa_2022_129059
crossref_primary_10_1016_j_ijbiomac_2024_134817
crossref_primary_10_3389_fonc_2023_1070069
crossref_primary_10_3390_medicina60030491
crossref_primary_10_1002_adfm_202425715
crossref_primary_10_1002_cctc_202400699
crossref_primary_10_1007_s12668_024_01405_0
crossref_primary_10_1016_j_ijbiomac_2024_139174
crossref_primary_10_1016_j_carbpol_2023_121414
crossref_primary_10_1016_j_procbio_2023_06_003
crossref_primary_10_1016_j_bcab_2024_103180
crossref_primary_10_3390_ijms25084174
crossref_primary_10_3390_catal13040780
crossref_primary_10_18311_jbc_2024_44037
crossref_primary_10_1007_s10562_023_04418_8
crossref_primary_10_1007_s43153_023_00432_w
crossref_primary_10_3390_biom13071156
crossref_primary_10_1016_j_jspr_2024_102468
crossref_primary_10_3390_nano12132303
crossref_primary_10_1007_s12668_024_01779_1
crossref_primary_10_1016_j_enzmictec_2023_110354
crossref_primary_10_3390_app15052637
crossref_primary_10_3390_ma17112774
Cites_doi 10.1016/j.ajps.2015.09.004
10.3109/02652040903131301
10.3390/ma12050704
10.1021/bm401341k
10.1021/acsami.6b13545
10.1590/fst.31518
10.1016/j.jddst.2020.102225
10.1016/j.ijpharm.2012.10.036
10.3390/polym12040832
10.1590/s2175-97902019000118736
10.1016/j.jddst.2020.102231
10.1007/978-1-62703-550-7_15
10.1016/S1367-5931(00)00182-4
10.1016/j.foodhyd.2019.01.062
10.3389/conf.FBIOE.2016.01.03002
10.1016/j.procbio.2021.02.018
10.1016/j.foodchem.2021.129325
10.1002/adma.200903411
10.1016/j.ijpharm.2018.05.037
10.1016/j.cej.2014.11.097
10.1371/journal.pone.0086785
10.1016/S0958-1669(02)00328-2
10.1155/2019/1354872
10.1007/s12010-017-2566-5
10.1016/j.carbpol.2020.116389
10.1016/j.foodhyd.2020.105855
10.1186/s42269-019-0148-0
10.1016/j.crfs.2021.06.003
10.1177/1082013217753898
10.3390/catal10091085
10.1590/0001-3765202020180609
10.1016/j.matpr.2020.12.922
10.1002/btpr.226
10.3390/ph13040063
10.1016/j.cis.2017.02.010
10.1007/s12275-019-8528-6
10.1590/0366-69132020663802922
10.1007/s13205-021-02748-1
10.1016/j.fbp.2019.02.002
10.1016/j.scitotenv.2016.09.215
10.1002/pat.3569
10.1016/j.msec.2020.110917
10.1016/j.pupt.2013.07.010
10.3390/catal10050489
10.1016/j.lwt.2021.111863
10.1016/j.ijpharm.2017.08.064
10.1016/j.msec.2016.05.121
10.1039/D1GC01852C
10.1002/adfm.201300320
10.1002/advs.201700513
10.3390/gels4030067
10.1163/156856201750180807
10.1080/10826068.2019.1709979
10.1163/156856209X444420
10.1016/j.jfoodeng.2018.09.016
10.1039/C3CS60075K
10.1007/s40883-018-0072-0
10.1016/j.rinphs.2012.08.001
10.1039/C4RA10239H
10.1021/acs.analchem.9b05466
10.1016/j.enzmictec.2005.12.002
10.1016/j.cofs.2015.05.009
10.1039/9781788013178
10.1016/j.progpolymsci.2011.06.003
10.1021/acs.langmuir.5b01442
10.1039/C7FO01721A
10.1016/j.foodhyd.2019.04.070
10.1016/j.foodhyd.2019.105536
10.1016/j.rinphs.2012.11.001
10.1208/s12248-019-0405-z
10.5757/ASCT.2017.26.6.157
10.7717/peerj.3665
10.1007/s10853-016-9932-5
10.1016/j.enzmictec.2006.08.023
10.1081/DRT-200054243
10.1016/B978-0-12-815665-0.00002-3
10.3389/fpsyg.2017.01850
10.3390/md13085156
10.3390/microorganisms9091857
10.1016/S0141-0229(01)00393-3
10.1007/s00449-005-0043-y
10.1007/s11483-011-9225-0
10.4103/0250-474X.65010
10.1186/1556-276X-9-340
10.1016/j.carbpol.2021.118076
10.3390/molecules21111577
10.1016/j.carbpol.2020.116568
10.1039/C5TC02080H
10.1201/b17280
10.1007/s00449-020-02489-0
10.1016/j.carres.2020.108004
10.1038/nature11117
10.3389/fbioe.2018.00212
10.1080/13102818.2015.1008192
10.1016/j.actbio.2017.12.014
10.3390/pharmaceutics13030329
10.3390/ijms19113393
10.1021/acsomega.0c06299
10.1016/j.ijpharm.2009.10.018
10.1016/j.ijpharm.2011.05.049
10.3906/biy-1805-28
10.1016/j.ijbiomac.2019.04.197
10.1016/j.molcatb.2012.02.005
10.1016/j.jconrel.2021.03.033
10.1016/j.lwt.2017.12.036
10.1007/s10853-010-4257-2
10.1016/j.idairyj.2006.01.005
10.1016/j.foodres.2007.07.004
10.1016/j.tifs.2018.05.018
10.3390/catal10080834
10.1016/j.procbio.2004.08.014
10.3109/03639045.2013.814060
10.1016/j.jconrel.2019.02.044
10.1021/bm4012776
10.1016/j.tifs.2016.10.019
10.1039/C4SC03367A
10.1016/j.colsurfb.2021.111583
10.1021/bm0700688
10.1007/978-3-319-41421-8
10.3390/mi9110562
10.1016/j.ijbiomac.2020.06.180
10.1007/s12010-018-2694-6
10.1021/acs.bioconjchem.8b00206
10.3390/polym13162666
10.1016/S0091-679X(07)84005-2
10.1016/j.carbpol.2019.115605
10.1155/2012/823830
10.1002/app.42125
10.1088/1755-1315/292/1/012028
10.1016/j.ijpharm.2006.05.059
10.1016/j.foodhyd.2016.06.003
10.1016/j.biomaterials.2020.120238
10.1016/j.ijpharm.2005.11.048
10.1080/87559129.2020.1733008
10.1016/j.ijbiomac.2016.01.079
10.1016/j.ijbiomac.2018.01.105
10.1016/j.proeng.2013.12.200
10.1016/j.carbpol.2016.12.033
10.1517/17425247.2011.553216
10.1002/jps.21886
10.1590/S0104-66322012000100002
10.1016/j.tifs.2021.01.040
10.1271/bbb.69.128
10.1590/S1516-89132003000200005
10.15171/apb.2017.017
10.1016/j.molcatb.2010.12.009
10.3390/polym13071105
10.1002/adfm.200800388
10.30638/eemj.2012.241
10.1351/pac199668122287
10.1016/j.jgeb.2012.03.003
10.1016/j.matchemphys.2011.04.043
10.1016/j.ijbiomac.2019.08.009
10.3109/02652048.2012.659286
10.1016/0378-5173(89)90281-0
10.1016/j.foostr.2016.10.003
10.1021/cs200124a
10.1016/j.envint.2019.01.011
10.1016/j.procbio.2019.11.026
10.1155/2015/145903
10.1016/j.carbpol.2013.07.032
10.1039/D0RE00109K
10.1088/1742-6596/1494/1/012028
10.1016/j.foodhyd.2016.10.022
10.1016/j.foodhyd.2017.01.005
10.1016/j.molcatb.2004.08.004
10.1007/978-1-4939-6364-5_7
10.1016/j.procbio.2005.01.028
10.1371/journal.pone.0047154
10.1016/j.jconrel.2012.12.008
10.1016/j.tifs.2016.10.012
10.1007/s00449-019-02164-z
10.1007/s12010-008-8233-0
10.1016/B978-0-12-819820-9.00024-7
10.1002/jps.20665
ContentType Journal Article
Copyright 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
2021 by the authors. 2021
Copyright_xml – notice: 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
– notice: 2021 by the authors. 2021
DBID AAYXX
CITATION
7SR
8FD
8FE
8FG
ABJCF
ABUWG
AFKRA
AZQEC
BENPR
BGLVJ
CCPQU
D1I
DWQXO
HCIFZ
JG9
KB.
PDBOC
PHGZM
PHGZT
PIMPY
PKEHL
PQEST
PQGLB
PQQKQ
PQUKI
PRINS
7X8
5PM
ADTOC
UNPAY
DOI 10.3390/polym13234061
DatabaseName CrossRef
Engineered Materials Abstracts
Technology Research Database
ProQuest SciTech Collection
ProQuest Technology Collection
Materials Science & Engineering Collection
ProQuest Central (Alumni)
ProQuest Central
ProQuest Central Essentials - QC
ProQuest Central
Technology Collection
ProQuest One Community College
ProQuest Materials Science Collection
ProQuest Central
SciTech Collection (ProQuest)
Materials Research Database
Materials Science Database
Materials Science Collection
Proquest Central Premium
ProQuest One Academic
Publicly Available Content Database
ProQuest One Academic Middle East (New)
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Applied & Life Sciences
ProQuest One Academic
ProQuest One Academic UKI Edition
ProQuest Central China
MEDLINE - Academic
PubMed Central (Full Participant titles)
Unpaywall for CDI: Periodical Content
Unpaywall
DatabaseTitle CrossRef
Publicly Available Content Database
Materials Research Database
Technology Collection
Technology Research Database
ProQuest One Academic Middle East (New)
ProQuest Central Essentials
Materials Science Collection
ProQuest Central (Alumni Edition)
SciTech Premium Collection
ProQuest One Community College
ProQuest Central China
ProQuest Central
ProQuest One Applied & Life Sciences
Engineered Materials Abstracts
ProQuest Central Korea
Materials Science Database
ProQuest Central (New)
ProQuest Materials Science Collection
ProQuest One Academic Eastern Edition
ProQuest Technology Collection
ProQuest SciTech Collection
ProQuest One Academic UKI Edition
Materials Science & Engineering Collection
ProQuest One Academic
ProQuest One Academic (New)
MEDLINE - Academic
DatabaseTitleList
MEDLINE - Academic
CrossRef
Publicly Available Content Database
Database_xml – sequence: 1
  dbid: UNPAY
  name: Unpaywall
  url: https://proxy.k.utb.cz/login?url=https://unpaywall.org/
  sourceTypes: Open Access Repository
– sequence: 2
  dbid: 8FG
  name: ProQuest Technology Collection
  url: https://search.proquest.com/technologycollection1
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Chemistry
EISSN 2073-4360
ExternalDocumentID 10.3390/polym13234061
PMC8659040
10_3390_polym13234061
GroupedDBID 53G
5VS
8FE
8FG
A8Z
AADQD
AAFWJ
AAYXX
ABDBF
ABJCF
ACGFO
ACIWK
ACUHS
ADBBV
ADMLS
AENEX
AFKRA
AFZYC
AIAGR
ALMA_UNASSIGNED_HOLDINGS
AOIJS
BCNDV
BENPR
BGLVJ
CCPQU
CITATION
CZ9
D1I
ESTFP
ESX
F5P
GX1
HCIFZ
HH5
HYE
I-F
IAO
ITC
KB.
KC.
KQ8
ML~
MODMG
M~E
OK1
PDBOC
PGMZT
PHGZM
PHGZT
PIMPY
PQGLB
PROAC
RNS
RPM
TR2
TUS
7SR
8FD
ABUWG
AZQEC
DWQXO
JG9
PKEHL
PQEST
PQQKQ
PQUKI
PRINS
7X8
PUEGO
5PM
ADTOC
C1A
IPNFZ
RIG
UNPAY
ID FETCH-LOGICAL-c392t-56559bddee5e9cc00d2a44a28dc6f7b10d6f3462ef8c1823facb70b78b6ee70a3
IEDL.DBID UNPAY
ISSN 2073-4360
IngestDate Sun Oct 26 03:35:11 EDT 2025
Tue Sep 30 15:56:29 EDT 2025
Thu Oct 02 10:43:30 EDT 2025
Fri Jul 25 12:04:47 EDT 2025
Thu Oct 16 04:31:32 EDT 2025
Thu Apr 24 23:04:03 EDT 2025
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 23
Language English
License Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
cc-by
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c392t-56559bddee5e9cc00d2a44a28dc6f7b10d6f3462ef8c1823facb70b78b6ee70a3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
ObjectType-Review-3
content type line 23
ORCID 0000-0001-8951-8639
0000-0002-8329-9241
0000-0001-9088-7431
OpenAccessLink https://proxy.k.utb.cz/login?url=https://www.mdpi.com/2073-4360/13/23/4061/pdf?version=1637663901
PMID 34883565
PQID 2608133954
PQPubID 2032345
ParticipantIDs unpaywall_primary_10_3390_polym13234061
pubmedcentral_primary_oai_pubmedcentral_nih_gov_8659040
proquest_miscellaneous_2608538374
proquest_journals_2608133954
crossref_primary_10_3390_polym13234061
crossref_citationtrail_10_3390_polym13234061
PublicationCentury 2000
PublicationDate 20211123
PublicationDateYYYYMMDD 2021-11-23
PublicationDate_xml – month: 11
  year: 2021
  text: 20211123
  day: 23
PublicationDecade 2020
PublicationPlace Basel
PublicationPlace_xml – name: Basel
PublicationTitle Polymers
PublicationYear 2021
Publisher MDPI AG
MDPI
Publisher_xml – name: MDPI AG
– name: MDPI
References Nguyen (ref_15) 2017; 26
Salleh (ref_123) 2014; 8
ref_137
ref_92
Jadhav (ref_90) 2013; 98
Lee (ref_46) 2012; 37
Tarhini (ref_176) 2017; 532
ref_133
Jenkins (ref_21) 1996; 68
ref_134
Kendall (ref_68) 2017; 1479
Long (ref_120) 2017; 5
Steinhilber (ref_140) 2013; 169
Won (ref_52) 2005; 40
Geonzon (ref_73) 2019; 92
ref_126
Pan (ref_194) 2017; 9
ref_127
Mendes (ref_179) 2017; 68
Samborska (ref_173) 2005; 23
Zusfahair (ref_58) 2020; 1494
Comunian (ref_165) 2016; 61
ref_121
Li (ref_124) 2016; 51
Shoba (ref_191) 2014; 4
Ataide (ref_138) 2021; 61
(ref_56) 2013; 2013
Karlsen (ref_45) 2002; 28
David (ref_71) 2018; 9
Kim (ref_83) 2019; 244
ref_72
Mendes (ref_78) 2020; 31
ref_158
Zheng (ref_74) 2020; 105
Zhang (ref_79) 2017; 67
Adzmi (ref_64) 2012; 29
Cascone (ref_28) 2001; 12
ref_156
Huo (ref_102) 2015; 6
Fredenberg (ref_181) 2011; 415
Abbasian (ref_23) 2019; 134
Vimal (ref_167) 2021; 61
Liao (ref_136) 2020; 257
ref_149
Boudrant (ref_20) 2020; 90
Wagner (ref_152) 2015; 26
Debele (ref_42) 2016; 68
Sankalia (ref_49) 2006; 312
ref_86
Bilal (ref_168) 2017; 575
Raza (ref_33) 2020; 492
Galliani (ref_146) 2018; 29
Wang (ref_135) 2021; 107
Yamazaki (ref_77) 2015; 278
Fraga (ref_2) 2021; 11
Bezerra (ref_39) 2015; 132
Shahid (ref_48) 2019; 2019
Vilgis (ref_110) 2015; 3
Patel (ref_132) 2013; 23
Gabrielczyk (ref_141) 2018; 185
Silva (ref_75) 2020; 92
Srikar (ref_190) 2019; 55
Griebenow (ref_147) 2012; 2
Sassolas (ref_101) 2013; 1051
Echegoyen (ref_178) 2017; 60
Mogharabi (ref_128) 2012; 2012
Eghbal (ref_187) 2018; 90
Camargo (ref_148) 2009; 20
Kita (ref_186) 2011; 8
Cargnin (ref_97) 2021; 150
Desai (ref_80) 2004; 31
Vieira (ref_105) 2011; 69
ref_114
Boostani (ref_182) 2021; 109
ref_117
ref_119
Mahajan (ref_103) 2010; 72
Bilal (ref_87) 2019; 124
Nordqvist (ref_109) 2011; 6
ref_112
Fessi (ref_183) 2010; 385
Amaral (ref_4) 2019; 115
Sharma (ref_188) 2016; 11
Cao (ref_85) 2020; 242
Bobone (ref_144) 2015; 31
ref_106
Imam (ref_99) 2021; 23
Freitas (ref_34) 2020; 66
Satar (ref_94) 2008; 67
Karamitros (ref_161) 2013; 14
Mak (ref_192) 2008; 18
Pedroche (ref_111) 2007; 40
Bourgeois (ref_91) 2006; 324
Khotimchenko (ref_70) 2020; 246
Mahajan (ref_31) 2011; 3
Ogueri (ref_24) 2019; 5
Mariod (ref_116) 2013; 12
Bornscheuer (ref_6) 2001; 5
Wardoyo (ref_81) 2019; 292
Brumano (ref_36) 2019; 6
Gharsallaoui (ref_170) 2007; 40
Freitas (ref_66) 2012; 29
Isa (ref_160) 2018; 67
Zaharaki (ref_29) 2010; 45
Chivers (ref_17) 2020; 5
ref_25
Liu (ref_139) 2011; 129
Prakash (ref_104) 2011; 13
Jaiswal (ref_130) 2012; 10
Fessi (ref_177) 1989; 55
ref_27
Bakry (ref_69) 2019; 96
Rahim (ref_65) 2013; 68
Karim (ref_113) 2021; 200
Raghu (ref_63) 2018; 42
Cardoso (ref_40) 2019; 39
Zheng (ref_88) 2020; 101
Osman (ref_16) 2013; 26
Labus (ref_122) 2016; 70
Alipal (ref_118) 2021; 42
Jaiswal (ref_169) 2016; 86
Nunes (ref_3) 2021; 44
Bornscheuer (ref_5) 2012; 485
Konsoula (ref_54) 2006; 41
Nishinari (ref_100) 2017; 13
Rabanel (ref_26) 2009; 25
Ghebremedhin (ref_107) 2021; 4
Konsoula (ref_53) 2006; 39
Hassan (ref_82) 2019; 43
Nagatomo (ref_129) 2005; 69
Basso (ref_7) 2019; 479
Diniz (ref_13) 2019; 139
Markwalter (ref_18) 2020; 22
Luraghi (ref_180) 2021; 334
Miao (ref_41) 2018; 5
Guo (ref_43) 2020; 162
Bahreini (ref_166) 2014; 9
Dey (ref_51) 2003; 46
Madalena (ref_142) 2017; 243
Arpagaus (ref_171) 2018; 546
ref_57
Sankalia (ref_50) 2006; 95
Kirk (ref_1) 2002; 13
Zhang (ref_131) 2012; 78
Chen (ref_98) 2021; 265
Patil (ref_164) 2010; 5
Edmans (ref_19) 2020; 112
Tran (ref_12) 2011; 1
Russ (ref_108) 2013; 14
Villalonga (ref_96) 2006; 28
Vishali (ref_175) 2019; 300
Sheldon (ref_10) 2013; 42
Aguiar (ref_143) 2016; 58
ref_162
ref_67
Malhotra (ref_76) 2020; 50
Yadav (ref_22) 2015; 4
Moriyama (ref_47) 2021; 6
Hosseini (ref_60) 2021; 352
(ref_61) 2018; 184
Ewadh (ref_125) 2009; 33
Rezakhani (ref_62) 2014; 5
Mohamad (ref_11) 2015; 29
Lindhoud (ref_155) 2007; 8
DeGroot (ref_59) 2001; 29
Yaghoobi (ref_153) 2017; 7
Cal (ref_172) 2010; 99
Cruz (ref_95) 2015; 2015
Tawfeek (ref_145) 2014; 40
Jyothi (ref_189) 2010; 27
Estevinho (ref_157) 2012; 11
ref_35
Demirkan (ref_55) 2011; 16
Mahmoud (ref_163) 2018; 24
Costas (ref_89) 2008; 151
ref_38
Orellano (ref_154) 2012; 2
Racine (ref_37) 2017; 8
Housseiny (ref_151) 2019; 57
Chan (ref_84) 2017; 161
Ma (ref_32) 2020; 230
Spink (ref_185) 2008; 84
ref_184
Sharma (ref_93) 2019; 42
Anjani (ref_14) 2007; 17
ref_44
Wang (ref_30) 2015; 3
Price (ref_193) 2010; 22
Sattar (ref_115) 2018; 111
Dhanjai (ref_150) 2020; 92
Tawfeek (ref_159) 2013; 441
Shishir (ref_174) 2018; 78
ref_9
ref_8
References_xml – volume: 11
  start-page: 404
  year: 2016
  ident: ref_188
  article-title: Effect of Process and Formulation Variables on the Preparation of Parenteral Paclitaxel-Loaded Biodegradable Polymeric Nanoparticles: A Co-Surfactant Study
  publication-title: Asian J. Pharm. Sci.
  doi: 10.1016/j.ajps.2015.09.004
– volume: 27
  start-page: 187
  year: 2010
  ident: ref_189
  article-title: Microencapsulation Techniques, Factors Influencing Encapsulation Efficiency
  publication-title: Artic. J. Microencapsul.
  doi: 10.3109/02652040903131301
– ident: ref_137
  doi: 10.3390/ma12050704
– volume: 14
  start-page: 4398
  year: 2013
  ident: ref_161
  article-title: Preserving Catalytic Activity and Enhancing Biochemical Stability of the Therapeutic Enzyme Asparaginase by Biocompatible Multilayered Polyelectrolyte Microcapsules
  publication-title: Biomacromolecules
  doi: 10.1021/bm401341k
– volume: 9
  start-page: 5447
  year: 2017
  ident: ref_194
  article-title: Engineering and Design of Polymeric Shells: Inwards Interweaving Polymers as Multilayer Nanofilm, Immobilization Matrix, or Chromatography Resins
  publication-title: ACS Appl. Mater. Interfaces
  doi: 10.1021/acsami.6b13545
– volume: 39
  start-page: 247
  year: 2019
  ident: ref_40
  article-title: Study of the Parameters Used in the Encapsulation of Commercial Pectinase in Calcium Alginate and Its Effect on Its Catalytic Activity
  publication-title: Food Sci. Technol.
  doi: 10.1590/fst.31518
– volume: 61
  start-page: 102225
  year: 2021
  ident: ref_138
  article-title: Freeze-Dried Chitosan Nanoparticles to Stabilize and Deliver Bromelain
  publication-title: J. Drug Deliv. Sci. Technol.
  doi: 10.1016/j.jddst.2020.102225
– volume: 441
  start-page: 611
  year: 2013
  ident: ref_159
  article-title: Dry Powder Inhalation of Macromolecules Using Novel PEG-Co-Polyester Microparticle Carriers
  publication-title: Int. J. Pharm.
  doi: 10.1016/j.ijpharm.2012.10.036
– ident: ref_149
  doi: 10.3390/polym12040832
– volume: 55
  start-page: e18736
  year: 2019
  ident: ref_190
  article-title: Study on Influence of Polymer and Surfactant on in Vitro Performance of Biodegradable Aqueous-Core Nanocapsules of Tenofovirdisoproxil Fumarate by Response Surface Methodology
  publication-title: Braz. J. Pharm. Sci.
  doi: 10.1590/s2175-97902019000118736
– volume: 61
  start-page: 102231
  year: 2021
  ident: ref_167
  article-title: Antimicrobial Potency Evaluation of Free and Immobilized L-Asparaginase Using Chitosan Nanoparticles
  publication-title: J. Drug Deliv. Sci. Technol.
  doi: 10.1016/j.jddst.2020.102231
– volume: 1051
  start-page: 229
  year: 2013
  ident: ref_101
  article-title: Enzyme Immobilization by Entrapment Within a Gel Network
  publication-title: Methods Mol. Biol.
  doi: 10.1007/978-1-62703-550-7_15
– volume: 5
  start-page: 137
  year: 2001
  ident: ref_6
  article-title: Improved Biocatalysts by Directed Evolution and Rational Protein Design
  publication-title: Curr. Opin. Chem. Biol.
  doi: 10.1016/S1367-5931(00)00182-4
– volume: 92
  start-page: 173
  year: 2019
  ident: ref_73
  article-title: Network Structure and Gelation Mechanism of Kappa and Iota Carrageenan Elucidated by Multiple Particle Tracking
  publication-title: Food Hydrocoll.
  doi: 10.1016/j.foodhyd.2019.01.062
– ident: ref_44
  doi: 10.3389/conf.FBIOE.2016.01.03002
– volume: 107
  start-page: 38
  year: 2021
  ident: ref_135
  article-title: Cellulase Immobilized by Sodium Alginate-Polyethylene Glycol-Chitosan for Hydrolysis Enhancement of Microcrystalline Cellulose
  publication-title: Process. Biochem.
  doi: 10.1016/j.procbio.2021.02.018
– volume: 352
  start-page: 129325
  year: 2021
  ident: ref_60
  article-title: Optimization of Microbial Rennet Encapsulation in Alginate—Chitosan Nanoparticles
  publication-title: Food Chem.
  doi: 10.1016/j.foodchem.2021.129325
– volume: 22
  start-page: 720
  year: 2010
  ident: ref_193
  article-title: A Biomolecular “Ship-in-a-bottle”: Continuous RNA Synthesis Within Hollow Polymer Hydrogel Assemblies
  publication-title: Adv. Mater.
  doi: 10.1002/adma.200903411
– volume: 546
  start-page: 194
  year: 2018
  ident: ref_171
  article-title: Nano Spray Drying for Encapsulation of Pharmaceuticals
  publication-title: Int. J. Pharm.
  doi: 10.1016/j.ijpharm.2018.05.037
– volume: 67
  start-page: 609
  year: 2008
  ident: ref_94
  article-title: Studies on Calcium Alginate-Pectin Gel Entrapped Concanavalin A-Bitter Gourd (Momordica Charantia) Peroxidase Complex
  publication-title: J. Sci. Ind. Res.
– volume: 278
  start-page: 122
  year: 2015
  ident: ref_77
  article-title: Flexible Film-Type Catalysts Encapsulating Urease within κ-Carrageenan Hydrogel Network
  publication-title: Chem. Eng. J.
  doi: 10.1016/j.cej.2014.11.097
– ident: ref_112
  doi: 10.1371/journal.pone.0086785
– volume: 13
  start-page: 345
  year: 2002
  ident: ref_1
  article-title: Industrial Enzyme Applications
  publication-title: Curr. Opin. Biotechnol.
  doi: 10.1016/S0958-1669(02)00328-2
– volume: 2019
  start-page: 1354872
  year: 2019
  ident: ref_48
  article-title: Immobilization of Dextranase Using Anionic Natural Polymer Alginate as a Matrix for the Degradation of a Long-Chain Biopolymer (Dextran)
  publication-title: Int. J. Polym. Sci.
  doi: 10.1155/2019/1354872
– volume: 184
  start-page: 538
  year: 2018
  ident: ref_61
  article-title: Optimization of Enzyme Co-Immobilization with Sodium Alginate and Glutaraldehyde-Activated Chitosan Beads
  publication-title: Appl. Biochem. Biotechnol.
  doi: 10.1007/s12010-017-2566-5
– volume: 242
  start-page: 116389
  year: 2020
  ident: ref_85
  article-title: Egg-Box Model-Based Gelation of Alginate and Pectin: A Review
  publication-title: Carbohydr. Polym.
  doi: 10.1016/j.carbpol.2020.116389
– volume: 105
  start-page: 105855
  year: 2020
  ident: ref_74
  article-title: Development of Food-Grade Bigels Based on κ-Carrageenan Hydrogel and Monoglyceride Oleogels as Carriers for β-Carotene: Roles of Oleogel Fraction
  publication-title: Food Hydrocoll.
  doi: 10.1016/j.foodhyd.2020.105855
– volume: 43
  start-page: 1
  year: 2019
  ident: ref_82
  article-title: Covalent Immobilization of Glucoamylase Enzyme onto Chemically Activated Surface of κ-Carrageenan
  publication-title: Bull. Natl. Res. Cent.
  doi: 10.1186/s42269-019-0148-0
– volume: 4
  start-page: 436
  year: 2021
  ident: ref_107
  article-title: Physics of Agarose Fluid Gels: Rheological Properties and Microstructure
  publication-title: Curr. Res. Food Sci.
  doi: 10.1016/j.crfs.2021.06.003
– volume: 24
  start-page: 330
  year: 2018
  ident: ref_163
  article-title: Micro- and Nano-Capsulated Fungal Pectinase with Outstanding Capabilities of Eliminating Turbidity in Freshly Produced Juice
  publication-title: Food Sci. Technol. Int.
  doi: 10.1177/1082013217753898
– ident: ref_158
  doi: 10.3390/catal10091085
– volume: 92
  start-page: 20180609
  year: 2020
  ident: ref_75
  article-title: β-Galactosidase Encapsulated in Carrageenan, Pectin and Carrageenan/Pectin: Comparative Study, Stability and Controlled Release
  publication-title: An. Acad. Bras. Ciências
  doi: 10.1590/0001-3765202020180609
– volume: 42
  start-page: 240
  year: 2021
  ident: ref_118
  article-title: A Review of Gelatin: Properties, Sources, Process, Applications, and Commercialisation
  publication-title: Mater. Today Proc.
  doi: 10.1016/j.matpr.2020.12.922
– volume: 25
  start-page: 946
  year: 2009
  ident: ref_26
  article-title: Progress Technology in Microencapsulation Methods for Cell Therapy
  publication-title: Biotechnol. Prog.
  doi: 10.1002/btpr.226
– volume: 4
  start-page: 119
  year: 2015
  ident: ref_22
  article-title: Microencapsulation Techniques Applicable To Food Flavours Research And Development: A Comprehensive Review
  publication-title: Int. J. Food Nutr. Sci.
– ident: ref_156
  doi: 10.3390/ph13040063
– volume: 243
  start-page: 23
  year: 2017
  ident: ref_142
  article-title: Micro- and Nano Bio-Based Delivery Systems for Food Applications: In Vitro Behavior
  publication-title: Adv. Colloid Interface Sci.
  doi: 10.1016/j.cis.2017.02.010
– volume: 57
  start-page: 521
  year: 2019
  ident: ref_151
  article-title: Nano-Encapsulation of Naringinase Produced by Trichoderma Longibrachiatum ATCC18648 on Thermally Stable Biopolymers for Citrus Juice Debittering
  publication-title: J. Microbiol.
  doi: 10.1007/s12275-019-8528-6
– volume: 66
  start-page: 421
  year: 2020
  ident: ref_34
  article-title: Tricalcium Phosphate Sheets with Chitosan Obtained via Aqueous Tape Casting
  publication-title: Cerâmica
  doi: 10.1590/0366-69132020663802922
– volume: 11
  start-page: 191
  year: 2021
  ident: ref_2
  article-title: Palm Oil Wastes as Feedstock for Lipase Production by Yarrowia lipolytica and Biocatalyst Application/Reuse
  publication-title: 3 Biotech
  doi: 10.1007/s13205-021-02748-1
– volume: 115
  start-page: 68
  year: 2019
  ident: ref_4
  article-title: Mango Agro-Industrial Wastes for Lipase Production from Yarrowia Lipolytica and the Potential of the Fermented Solid as a Biocatalyst
  publication-title: Food Bioprod. Process.
  doi: 10.1016/j.fbp.2019.02.002
– volume: 575
  start-page: 1352
  year: 2017
  ident: ref_168
  article-title: Enhanced Bio-Catalytic Performance and Dye Degradation Potential of Chitosan-Encapsulated Horseradish Peroxidase in a Packed Bed Reactor System
  publication-title: Sci. Total. Environ.
  doi: 10.1016/j.scitotenv.2016.09.215
– volume: 26
  start-page: 1461
  year: 2015
  ident: ref_152
  article-title: Stable Formulation of Protein-Type Drug in Electrospun Polymeric Fiber Followed by Tableting and Scaling-up Experiments
  publication-title: Polym. Adv. Technol.
  doi: 10.1002/pat.3569
– volume: 112
  start-page: 110917
  year: 2020
  ident: ref_19
  article-title: Incorporation of Lysozyme into a Mucoadhesive Electrospun Patch for Rapid Protein Delivery to the Oral Mucosa
  publication-title: Mater. Sci. Eng. C
  doi: 10.1016/j.msec.2020.110917
– volume: 26
  start-page: 700
  year: 2013
  ident: ref_16
  article-title: Inhalable DNase I Microparticles Engineered with Biologically Active Excipients
  publication-title: Pulm. Pharmacol. Ther.
  doi: 10.1016/j.pupt.2013.07.010
– ident: ref_67
  doi: 10.3390/catal10050489
– volume: 150
  start-page: 111863
  year: 2021
  ident: ref_97
  article-title: Performance of Lactase Encapsulated in Pectin-Based Hydrogels during Lactose Hydrolysis Reactions
  publication-title: LWT
  doi: 10.1016/j.lwt.2021.111863
– volume: 532
  start-page: 66
  year: 2017
  ident: ref_176
  article-title: Nanoprecipitation Process: From Encapsulation to Drug Delivery
  publication-title: Int. J. Pharm.
  doi: 10.1016/j.ijpharm.2017.08.064
– volume: 68
  start-page: 964
  year: 2016
  ident: ref_42
  article-title: Polysaccharide based nanogels in the drug delivery system: Application as the carrier of pharmaceutical agents
  publication-title: Mater. Sci. Eng. C
  doi: 10.1016/j.msec.2016.05.121
– volume: 23
  start-page: 4980
  year: 2021
  ident: ref_99
  article-title: Enzyme Entrapment, Biocatalyst Immobilization without Covalent Attachment
  publication-title: Green Chemistry
  doi: 10.1039/D1GC01852C
– volume: 23
  start-page: 4710
  year: 2013
  ident: ref_132
  article-title: Novel All-Natural Microcapsules from Gelatin and Shellac for Biorelated Applications
  publication-title: Adv. Funct. Mater.
  doi: 10.1002/adfm.201300320
– volume: 5
  start-page: 1700513
  year: 2018
  ident: ref_41
  article-title: Polysaccharide-Based Controlled Release Systems for Therapeutics Delivery and Tissue Engineering: From Bench to Bedside
  publication-title: Adv. Sci.
  doi: 10.1002/advs.201700513
– ident: ref_38
  doi: 10.3390/gels4030067
– volume: 12
  start-page: 135
  year: 2013
  ident: ref_116
  article-title: Review: Gelatin, Source, Extraction and Industrial Applications
  publication-title: Acta Svi. Pol. Technol. Aliment.
– volume: 12
  start-page: 267
  year: 2001
  ident: ref_28
  article-title: Bioartificial Polymeric Materials Based on Polysaccharides
  publication-title: J. Biomater. Sci. Polym. Ed.
  doi: 10.1163/156856201750180807
– volume: 50
  start-page: 494
  year: 2020
  ident: ref_76
  article-title: Immobilization of Invertase in Calcium Alginate and Calcium Alginate-Kappa-Carrageenan Beads and Its Application in Bioethanol Production
  publication-title: Prep. Biochem. Biotechnol.
  doi: 10.1080/10826068.2019.1709979
– volume: 20
  start-page: 1065
  year: 2009
  ident: ref_148
  article-title: Nanoparticles Made of Microbial Poly(γ-Glutamate)s for Encapsulation and Delivery of Drugs and Proteins
  publication-title: J. Biomater. Sci. Polym. Ed.
  doi: 10.1163/156856209X444420
– volume: 244
  start-page: 159
  year: 2019
  ident: ref_83
  article-title: Analysis and Model-Based Optimization of a Pectin Extraction Process
  publication-title: J. Food Eng.
  doi: 10.1016/j.jfoodeng.2018.09.016
– volume: 42
  start-page: 6223
  year: 2013
  ident: ref_10
  article-title: Enzyme Immobilisation in Biocatalysis: Why, What and How
  publication-title: Chem. Soc. Rev.
  doi: 10.1039/C3CS60075K
– volume: 5
  start-page: 128
  year: 2019
  ident: ref_24
  article-title: Polymeric Biomaterials For Scaffold-Based Bone Regenerative Engineering
  publication-title: Regen. Eng. Transl. Med.
  doi: 10.1007/s40883-018-0072-0
– volume: 16
  start-page: 6690
  year: 2011
  ident: ref_55
  article-title: Immobilization of B. Amyloliquefaciens α-Amylase and Comparison of Some of Its Enzymatic Properties with the Free Form
  publication-title: Rom. Biotechnol. Lett.
– volume: 2
  start-page: 46
  year: 2012
  ident: ref_147
  article-title: Glycosylation Improves α-Chymotrypsin Stability upon Encapsulation in Poly(Lactic-Co-Glycolic)Acid Microspheres
  publication-title: Results Pharma Sci.
  doi: 10.1016/j.rinphs.2012.08.001
– volume: 4
  start-page: 60209
  year: 2014
  ident: ref_191
  article-title: Design and Development of Papain–Urea Loaded PVA Nanofibers for Wound Debridement
  publication-title: RSC Adv.
  doi: 10.1039/C4RA10239H
– volume: 92
  start-page: 5830
  year: 2020
  ident: ref_150
  article-title: Robust Single-Molecule Enzyme Nanocapsules for Biosensing with Significantly Improved Biosensor Stability
  publication-title: Anal. Chem.
  doi: 10.1021/acs.analchem.9b05466
– volume: 39
  start-page: 690
  year: 2006
  ident: ref_53
  article-title: Thermostable α-Amylase Production by Bacillus Subtilis Entrapped in Calcium Alginate Gel Capsules
  publication-title: Enzym. Microb. Technol.
  doi: 10.1016/j.enzmictec.2005.12.002
– volume: 3
  start-page: 71
  year: 2015
  ident: ref_110
  article-title: Gels: Model Systems for Soft Matter Food Physics
  publication-title: Curr. Opin. Food Sci.
  doi: 10.1016/j.cofs.2015.05.009
– ident: ref_119
  doi: 10.1039/9781788013178
– volume: 37
  start-page: 106
  year: 2012
  ident: ref_46
  article-title: Alginate: Properties and Biomedical Applications
  publication-title: Prog. Polym. Sci.
  doi: 10.1016/j.progpolymsci.2011.06.003
– volume: 31
  start-page: 7572
  year: 2015
  ident: ref_144
  article-title: Liposome-Templated Hydrogel Nanoparticles as Vehicles for Enzyme-Based Therapies
  publication-title: Langmuir
  doi: 10.1021/acs.langmuir.5b01442
– volume: 9
  start-page: 1344
  year: 2018
  ident: ref_71
  article-title: Revisiting the Carrageenan Controversy: Do We Really Understand the Digestive Fate and Safety of Carrageenan in Our Foods?
  publication-title: Food Funct.
  doi: 10.1039/C7FO01721A
– volume: 31
  start-page: 320
  year: 2020
  ident: ref_78
  article-title: Preparation and Delayed Release Study on Pancreatin Encapsulated into Alginate, Carrageenan and Pectin Hydrogels
  publication-title: J. Braz. Chem. Soc.
– volume: 96
  start-page: 43
  year: 2019
  ident: ref_69
  article-title: Myofibrillar Protein with κ- or λ-Carrageenans as Novel Shell Materials for Microencapsulation of Tuna Oil through Complex Coacervation
  publication-title: Food Hydrocoll.
  doi: 10.1016/j.foodhyd.2019.04.070
– volume: 101
  start-page: 105536
  year: 2020
  ident: ref_88
  article-title: Gelling Mechanism of RG-I Enriched Citrus Pectin: Role of Arabinose Side-Chains in Cation- and Acid-Induced Gelation
  publication-title: Food Hydrocoll.
  doi: 10.1016/j.foodhyd.2019.105536
– volume: 2
  start-page: 79
  year: 2012
  ident: ref_154
  article-title: Two-Step Nanoprecipitation for the Production of Protein-Loaded PLGA Nanospheres
  publication-title: Results Pharma Sci.
  doi: 10.1016/j.rinphs.2012.11.001
– volume: 22
  start-page: 1
  year: 2020
  ident: ref_18
  article-title: Polymeric Nanocarrier Formulations of Biologics Using Inverse Flash NanoPrecipitation
  publication-title: AAPS J.
  doi: 10.1208/s12248-019-0405-z
– volume: 26
  start-page: 157
  year: 2017
  ident: ref_15
  article-title: An Overview of Techniques in Enzyme Immobilization
  publication-title: Appl. Sci. Converg. Technol.
  doi: 10.5757/ASCT.2017.26.6.157
– volume: 5
  start-page: e3665
  year: 2017
  ident: ref_120
  article-title: Preparation and Characteristics of Gelatin Sponges Crosslinked by Microbial Transglutaminase
  publication-title: PeerJ
  doi: 10.7717/peerj.3665
– volume: 51
  start-page: 6357
  year: 2016
  ident: ref_124
  article-title: Immobilizing Enzymes in Regular-Sized Gelatin Microspheres through a Membrane Emulsification Method
  publication-title: J. Mater. Sci.
  doi: 10.1007/s10853-016-9932-5
– volume: 40
  start-page: 1160
  year: 2007
  ident: ref_111
  article-title: Effect of the Support and Experimental Conditions in the Intensity of the Multipoint Covalent Attachment of Proteins on Glyoxyl-Agarose Supports: Correlation between Enzyme–Support Linkages and Thermal Stability
  publication-title: Enzym. Microb. Technol.
  doi: 10.1016/j.enzmictec.2006.08.023
– volume: 23
  start-page: 941
  year: 2005
  ident: ref_173
  article-title: Spray-Drying of α-Amylase—The Effect of Process Variables on the Enzyme Inactivation
  publication-title: Dry. Technol.
  doi: 10.1081/DRT-200054243
– ident: ref_9
  doi: 10.1016/B978-0-12-815665-0.00002-3
– volume: 8
  start-page: 1850
  year: 2017
  ident: ref_37
  article-title: Free Will and the Brain Disease Model of Addiction: The Not So Seductive Allure of Neuroscience and Its Modest Impact on the Attribution of Free Will to People with an Addiction
  publication-title: Front. Psychol.
  doi: 10.3389/fpsyg.2017.01850
– ident: ref_35
  doi: 10.3390/md13085156
– ident: ref_114
  doi: 10.3390/microorganisms9091857
– volume: 29
  start-page: 321
  year: 2001
  ident: ref_59
  article-title: Encapsulation of Urease in Alginate Beads and Protection from α-Chymotrypsin with Chitosan Membranes
  publication-title: Enzym. Microb. Technol.
  doi: 10.1016/S0141-0229(01)00393-3
– volume: 28
  start-page: 387
  year: 2006
  ident: ref_96
  article-title: Polyelectrolyte Complex Formation Mediated Immobilization of Chitosan-Invertase Neoglycoconjugate on Pectin-Coated Chitin
  publication-title: Bioprocess. Biosyst. Eng.
  doi: 10.1007/s00449-005-0043-y
– volume: 6
  start-page: 450
  year: 2011
  ident: ref_109
  article-title: Rheological Study of the Gelation Process of Agarose-Based Solutions
  publication-title: Food Biophys.
  doi: 10.1007/s11483-011-9225-0
– volume: 8
  start-page: 696
  year: 2014
  ident: ref_123
  article-title: Optimization of Spray Drying Process Conditions for Recombinant Stem Bromelain
  publication-title: Adv. Environ. Biol.
– volume: 72
  start-page: 223
  year: 2010
  ident: ref_103
  article-title: Comparison and Suitability of Gel Matrix for Entrapping Higher Content of Enzymes for Commercial Applications
  publication-title: Indian, J. Pharm. Sci.
  doi: 10.4103/0250-474X.65010
– ident: ref_133
– volume: 9
  start-page: 1
  year: 2014
  ident: ref_166
  article-title: Preparation and Nanoencapsulation of L-Asparaginase II in Chitosan-Tripolyphosphate Nanoparticles and in Vitro Release Study
  publication-title: Nanoscale Res. Lett.
  doi: 10.1186/1556-276X-9-340
– volume: 265
  start-page: 118076
  year: 2021
  ident: ref_98
  article-title: Agar Oligosaccharides: A Review of Preparation, Structures, Bioactivities and Application
  publication-title: Carbohydr. Polym.
  doi: 10.1016/j.carbpol.2021.118076
– ident: ref_106
  doi: 10.3390/molecules21111577
– ident: ref_117
– volume: 246
  start-page: 116568
  year: 2020
  ident: ref_70
  article-title: Antitumor Potential of Carrageenans from Marine Red Algae
  publication-title: Carbohydr. Polym.
  doi: 10.1016/j.carbpol.2020.116568
– volume: 3
  start-page: 10055
  year: 2015
  ident: ref_30
  article-title: Recent Progress in Organic Resistance Memory with Small Molecules and Inorganic–Organic Hybrid Polymers as Active Elements
  publication-title: J. Mater. Chem. C
  doi: 10.1039/C5TC02080H
– ident: ref_8
  doi: 10.1201/b17280
– volume: 2013
  start-page: 928913
  year: 2013
  ident: ref_56
  article-title: Immobilization and biochemical properties of the enantioselective recombinant NStcI esterase of Aspergillus nidulans
  publication-title: Enzym. Res.
– volume: 44
  start-page: 809
  year: 2021
  ident: ref_3
  article-title: Waste Soybean Frying Oil for the Production, Extraction, and Characterization of Cell-Wall-Associated Lipases from Yarrowia lipolytica
  publication-title: Bioprocess Biosyst. Eng.
  doi: 10.1007/s00449-020-02489-0
– volume: 492
  start-page: 108004
  year: 2020
  ident: ref_33
  article-title: Recent Developments in Chitosan Encapsulation of Various Active Ingredients for Multifunctional Applications
  publication-title: Carbohydr. Res.
  doi: 10.1016/j.carres.2020.108004
– volume: 485
  start-page: 185
  year: 2012
  ident: ref_5
  article-title: Engineering the Third Wave of Biocatalysis
  publication-title: Nature
  doi: 10.1038/nature11117
– volume: 6
  start-page: 212
  year: 2019
  ident: ref_36
  article-title: Development of L-Asparaginase Biobetters: Current Research Status and Review of the Desirable Quality Profiles
  publication-title: Front. Bioeng. Biotechnol.
  doi: 10.3389/fbioe.2018.00212
– volume: 29
  start-page: 205
  year: 2015
  ident: ref_11
  article-title: An Overview of Technologies for Immobilization of Enzymes and Surface Analysis Techniques for Immobilized Enzymes
  publication-title: Biotechnol. Biotechnol. Equip.
  doi: 10.1080/13102818.2015.1008192
– volume: 70
  start-page: 523
  year: 2016
  ident: ref_122
  article-title: Preparation and Characterisation of Gelatine Hydrogels Predisposed to Use as Matrices for Effective Immobilisation of Biocatalystst
  publication-title: Chem. Pap.
– volume: 67
  start-page: 21
  year: 2018
  ident: ref_160
  article-title: Antioxidant Functionalized Polymer Capsules to Prevent Oxidative Stress
  publication-title: Acta Biomater.
  doi: 10.1016/j.actbio.2017.12.014
– ident: ref_162
  doi: 10.3390/pharmaceutics13030329
– ident: ref_57
  doi: 10.3390/ijms19113393
– volume: 6
  start-page: 6368
  year: 2021
  ident: ref_47
  article-title: Efficient Entrapment of Carbonic Anhydrase in Alginate Hydrogels Using Liposomes for Continuous-Flow Catalytic Reactions
  publication-title: ACS Omega
  doi: 10.1021/acsomega.0c06299
– volume: 385
  start-page: 113
  year: 2010
  ident: ref_183
  article-title: Polymer-Based Nanocapsules for Drug Delivery
  publication-title: Int. J. Pharm.
  doi: 10.1016/j.ijpharm.2009.10.018
– volume: 415
  start-page: 34
  year: 2011
  ident: ref_181
  article-title: The Mechanisms of Drug Release in Poly(Lactic-Co-Glycolic Acid)-Based Drug Delivery Systems—A Review
  publication-title: Int. J. Pharm.
  doi: 10.1016/j.ijpharm.2011.05.049
– volume: 5
  start-page: 108
  year: 2014
  ident: ref_62
  article-title: Immobilization of Protease in Biopolymers (Mixture of Alginate-Chitosan)
  publication-title: J. Paramed. Sci.
– volume: 42
  start-page: 307
  year: 2018
  ident: ref_63
  article-title: Enhancing the Stability of a Carboxylesterase by Entrapment in Chitosan Coated Alginate Beads
  publication-title: Turk. J. Biol.
  doi: 10.3906/biy-1805-28
– volume: 134
  start-page: 673
  year: 2019
  ident: ref_23
  article-title: Scaffolding Polymeric Biomaterials: Are Naturally Occurring Biological Macromolecules More Appropriate for Tissue Engineering?
  publication-title: Int. J. Biol. Macromol.
  doi: 10.1016/j.ijbiomac.2019.04.197
– ident: ref_27
– volume: 78
  start-page: 65
  year: 2012
  ident: ref_131
  article-title: Enhancement of Activity and Stability of Lipase by Microemulsion-Based Organogels (MBGs) Immobilization and Application for Synthesis of Arylethyl Acetate
  publication-title: J. Mol. Catal. B Enzym.
  doi: 10.1016/j.molcatb.2012.02.005
– volume: 334
  start-page: 463
  year: 2021
  ident: ref_180
  article-title: Electrospinning for Drug Delivery Applications: A Review
  publication-title: J. Control. Release
  doi: 10.1016/j.jconrel.2021.03.033
– volume: 90
  start-page: 254
  year: 2018
  ident: ref_187
  article-title: Complex Coacervation: Encapsulation and Controlled Release of Active Agents in Food Systems
  publication-title: LWT
  doi: 10.1016/j.lwt.2017.12.036
– volume: 45
  start-page: 2715
  year: 2010
  ident: ref_29
  article-title: Use of Analytical Techniques for Identification of Inorganic Polymer Gel Composition
  publication-title: J. Mater. Sci.
  doi: 10.1007/s10853-010-4257-2
– volume: 17
  start-page: 79
  year: 2007
  ident: ref_14
  article-title: Microencapsulation of Enzymes for Potential Application in Acceleration of Cheese Ripening
  publication-title: Int. Dairy J.
  doi: 10.1016/j.idairyj.2006.01.005
– volume: 40
  start-page: 1107
  year: 2007
  ident: ref_170
  article-title: Applications of Spray-Drying in Microencapsulation of Food Ingredients: An Overview
  publication-title: Food Res. Int.
  doi: 10.1016/j.foodres.2007.07.004
– volume: 78
  start-page: 34
  year: 2018
  ident: ref_174
  article-title: Advances in Micro and Nano-Encapsulation of Bioactive Compounds Using Biopolymer and Lipid-Based Transporters
  publication-title: Trends Food Sci. Technol.
  doi: 10.1016/j.tifs.2018.05.018
– ident: ref_92
  doi: 10.3390/catal10080834
– volume: 40
  start-page: 2149
  year: 2005
  ident: ref_52
  article-title: Optimization of Lipase Entrapment in Ca-Alginate Gel Beads
  publication-title: Process Biochem.
  doi: 10.1016/j.procbio.2004.08.014
– volume: 40
  start-page: 1213
  year: 2014
  ident: ref_145
  article-title: Evaluation of Biodegradable Polyester-Co-Lactone Microparticles for Protein Delivery
  publication-title: Drug Dev. Ind. Pharm.
  doi: 10.3109/03639045.2013.814060
– volume: 300
  start-page: 93
  year: 2019
  ident: ref_175
  article-title: Spray freeze drying: Emerging applications in drug delivery
  publication-title: J. Control. Release
  doi: 10.1016/j.jconrel.2019.02.044
– volume: 14
  start-page: 4116
  year: 2013
  ident: ref_108
  article-title: Influence of Nongelling Hydrocolloids on the Gelation of Agarose
  publication-title: Biomacromolecules
  doi: 10.1021/bm4012776
– ident: ref_134
– volume: 60
  start-page: 71
  year: 2017
  ident: ref_178
  article-title: High Throughput Electro-Hydrodynamic Processing in Food Encapsulation and Food Packaging Applications: Viewpoint
  publication-title: Trends Food Sci. Technol.
  doi: 10.1016/j.tifs.2016.10.019
– volume: 6
  start-page: 1938
  year: 2015
  ident: ref_102
  article-title: Magnetic MOF Microreactors for Recyclable Size-Selective Biocatalysis
  publication-title: Chem. Sci.
  doi: 10.1039/C4SC03367A
– volume: 200
  start-page: 111583
  year: 2021
  ident: ref_113
  article-title: Single Step Immobilization of CMCase within Agarose Gel Matrix: Kinetics and Thermodynamic Studies
  publication-title: Colloids Surf. B Biointerfaces
  doi: 10.1016/j.colsurfb.2021.111583
– volume: 8
  start-page: 2219
  year: 2007
  ident: ref_155
  article-title: Structure and Stability of Complex Coacervate Core Micelles with Lysozyme
  publication-title: Biomacromolecules
  doi: 10.1021/bm0700688
– ident: ref_184
  doi: 10.1007/978-3-319-41421-8
– ident: ref_121
  doi: 10.3390/mi9110562
– volume: 162
  start-page: 618
  year: 2020
  ident: ref_43
  article-title: Structures, Properties and Application of Alginic Acid: A Review
  publication-title: Int. J. Biol. Macromol.
  doi: 10.1016/j.ijbiomac.2020.06.180
– volume: 185
  start-page: 847
  year: 2018
  ident: ref_141
  article-title: A Comparative Study on Immobilization of Fructosyltransferase in Biodegradable Polymers by Electrospinning
  publication-title: Appl. Biochem. Biotechnol.
  doi: 10.1007/s12010-018-2694-6
– volume: 29
  start-page: 2225
  year: 2018
  ident: ref_146
  article-title: Cross-Linked Enzyme Aggregates as Versatile Tool for Enzyme Delivery: Application to Polymeric Nanoparticles
  publication-title: Bioconjugate Chem.
  doi: 10.1021/acs.bioconjchem.8b00206
– ident: ref_72
  doi: 10.3390/polym13162666
– volume: 84
  start-page: 115
  year: 2008
  ident: ref_185
  article-title: Differential Scanning Calorimetry
  publication-title: Methods Cell Biol.
  doi: 10.1016/S0091-679X(07)84005-2
– volume: 230
  start-page: 115605
  year: 2020
  ident: ref_32
  article-title: Dissolution and Deacetylation of Chitin in Ionic Liquid Tetrabutylammonium Hydroxide and Its Cascade Reaction in Enzyme Treatment for Chitin Recycling
  publication-title: Carbohydr. Polym.
  doi: 10.1016/j.carbpol.2019.115605
– volume: 2012
  start-page: 823830
  year: 2012
  ident: ref_128
  article-title: Immobilization of Laccase in Alginate-Gelatin Mixed Gel and Decolorization of Synthetic Dyes
  publication-title: Bioinorg. Chem. Appl.
  doi: 10.1155/2012/823830
– volume: 132
  start-page: 42125
  year: 2015
  ident: ref_39
  article-title: Enzyme Immobilization onto Renewable Polymeric Matrixes: Past, Present, and Future Trends
  publication-title: J. Appl. Polym. Sci.
  doi: 10.1002/app.42125
– volume: 292
  start-page: 012028
  year: 2019
  ident: ref_81
  article-title: Thermal and Reused Stability of Immobilized Lipase in Carrageenan
  publication-title: IOP Conf. Ser. Earth Environ. Sci.
  doi: 10.1088/1755-1315/292/1/012028
– volume: 324
  start-page: 2
  year: 2006
  ident: ref_91
  article-title: Evaluation of Critical Formulation Parameters Influencing the Bioactivity of β-Lactamases Entrapped in Pectin Beads
  publication-title: Int. J. Pharm.
  doi: 10.1016/j.ijpharm.2006.05.059
– volume: 61
  start-page: 442
  year: 2016
  ident: ref_165
  article-title: Microencapsulation Using Biopolymers as an Alternative to Produce Food Enhanced with Phytosterols and Omega-3 Fatty Acids: A Review
  publication-title: Food Hydrocoll.
  doi: 10.1016/j.foodhyd.2016.06.003
– volume: 3
  start-page: 16
  year: 2011
  ident: ref_31
  article-title: Smart Polymers: Innovations In Novel Drug Delivery
  publication-title: Int. J. Drug Dev. Res.
– volume: 33
  start-page: 131
  year: 2009
  ident: ref_125
  article-title: Immobilization of Urease in Gelatin Beads for Urea Estimation
  publication-title: Natl. J. Chem.
– volume: 257
  start-page: 120238
  year: 2020
  ident: ref_136
  article-title: Enzymatic Protection and Biocompatibility Screening of Enzyme-Loaded Polymeric Nanoparticles for Neurotherapeutic Applications
  publication-title: Biomaterials
  doi: 10.1016/j.biomaterials.2020.120238
– volume: 312
  start-page: 1
  year: 2006
  ident: ref_49
  article-title: Stability Improvement of Alpha-Amylase Entrapped in Kappa-Carrageenan Beads: Physicochemical Characterization and Optimization Using Composite Index
  publication-title: Int. J. Pharm.
  doi: 10.1016/j.ijpharm.2005.11.048
– ident: ref_86
  doi: 10.1080/87559129.2020.1733008
– volume: 5
  start-page: 241
  year: 2010
  ident: ref_164
  article-title: Ionotropic Gelation And Polyelectrolyte Complexation: The Novel Techniques To Design Hydrogel Particulate Sustained, Modulated Drug Delivery System: A Review
  publication-title: Dig. J. Nanomater. Biostructures
– volume: 479
  start-page: 6437
  year: 2019
  ident: ref_7
  article-title: Industrial Applications of Immobilized Enzymes—A Review
  publication-title: Mol. Catal.
– volume: 86
  start-page: 288
  year: 2016
  ident: ref_169
  article-title: Immobilization of Papaya Laccase in Chitosan Led to Improved Multipronged Stability and Dye Discoloration
  publication-title: Int. J. Biol. Macromol.
  doi: 10.1016/j.ijbiomac.2016.01.079
– volume: 111
  start-page: 917
  year: 2018
  ident: ref_115
  article-title: Agar-Agar Immobilization: An Alternative Approach for the Entrapment of Protease to Improve the Catalytic Efficiency, Thermal Stability and Recycling Efficiency
  publication-title: Int. J. Biol. Macromol.
  doi: 10.1016/j.ijbiomac.2018.01.105
– volume: 68
  start-page: 411
  year: 2013
  ident: ref_65
  article-title: Enzymes Encapsulation within Calcium Alginate-Clay Beads: Characterization and Application for Cassava Slurry Saccharification
  publication-title: Procedia Eng.
  doi: 10.1016/j.proeng.2013.12.200
– volume: 161
  start-page: 118
  year: 2017
  ident: ref_84
  article-title: Pectin as a Rheology Modifier: Origin, Structure, Commercial Production and Rheology
  publication-title: Carbohydr. Polym.
  doi: 10.1016/j.carbpol.2016.12.033
– volume: 8
  start-page: 329
  year: 2011
  ident: ref_186
  article-title: Drug Delivery Vehicles with Improved Encapsulation Efficiency: Taking Advantage of Specific Drug-Carrier Interactions
  publication-title: Expert Opin. Drug Deliv.
  doi: 10.1517/17425247.2011.553216
– volume: 99
  start-page: 575
  year: 2010
  ident: ref_172
  article-title: Spray Drying Technique. I: Hardware and Process Parameters
  publication-title: J. Pharm. Sci.
  doi: 10.1002/jps.21886
– volume: 29
  start-page: 15
  year: 2012
  ident: ref_66
  article-title: Optimization of the Immobilization Process of β-Galatosidade by Combined Entrapment-Cross-Linking and the Kinetics of Lactose Hydrolysis
  publication-title: Braz. J. Chem. Eng.
  doi: 10.1590/S0104-66322012000100002
– volume: 109
  start-page: 303
  year: 2021
  ident: ref_182
  article-title: A Comprehensive Review on the Controlled Release of Encapsulated Food Ingredients; Fundamental Concepts to Design and Applications
  publication-title: Trends Food Sci. Technol.
  doi: 10.1016/j.tifs.2021.01.040
– volume: 69
  start-page: 128
  year: 2005
  ident: ref_129
  article-title: Preparation and Properties of Gelatin-Immobilized β-Glucosidase from Pyrococcus Furiosus
  publication-title: Biosci. Biotechnol. Biochem.
  doi: 10.1271/bbb.69.128
– volume: 46
  start-page: 167
  year: 2003
  ident: ref_51
  article-title: Immobilization of Alpha-Amylase Produced by Bacillus Circulans GRS 313
  publication-title: Braz. Arch. Biol. Technol.
  doi: 10.1590/S1516-89132003000200005
– volume: 13
  start-page: 572
  year: 2011
  ident: ref_104
  article-title: Immobilization of a Thermostable-Amylase on Agarose and Agar Matrices and Its Application in Starch Stain Removal
  publication-title: World Appl. Sci. J.
– volume: 7
  start-page: 131
  year: 2017
  ident: ref_153
  article-title: Preparation, Optimization and Activity Evaluation of PLGA/Streptokinase Nanoparticles Using Electrospray
  publication-title: Adv. Pharm. Bull.
  doi: 10.15171/apb.2017.017
– volume: 69
  start-page: 47
  year: 2011
  ident: ref_105
  article-title: β-Glucosidase Immobilized and Stabilized on Agarose Matrix Functionalized with Distinct Reactive Groups
  publication-title: J. Mol. Catal. B Enzym.
  doi: 10.1016/j.molcatb.2010.12.009
– ident: ref_25
  doi: 10.3390/polym13071105
– volume: 18
  start-page: 2930
  year: 2008
  ident: ref_192
  article-title: Diffusion Controlled and Temperature Stable Microcapsule Reaction Compartments for High-Throughput Microcapsule-PCR
  publication-title: Adv. Funct. Mater.
  doi: 10.1002/adfm.200800388
– volume: 11
  start-page: 1923
  year: 2012
  ident: ref_157
  article-title: Study of the Inhibition Effect on the Microencapsulated Enzyme β-Galactosidase
  publication-title: Environ. Eng. Manag. J.
  doi: 10.30638/eemj.2012.241
– volume: 68
  start-page: 2287
  year: 1996
  ident: ref_21
  article-title: Glossary of Basic Terms in Polymer Science (IUPAC Recommendations 1996)
  publication-title: Pure Appl. Chem.
  doi: 10.1351/pac199668122287
– volume: 10
  start-page: 161
  year: 2012
  ident: ref_130
  article-title: A-Amylase Immobilization on Gelatin: Optimization of Process Variables
  publication-title: J. Genet. Eng. Biotechnol.
  doi: 10.1016/j.jgeb.2012.03.003
– volume: 129
  start-page: 488
  year: 2011
  ident: ref_139
  article-title: Enzyme Encapsulation in Freeze-Dried Bionanocomposites Prepared from Chitosan and Xanthan Gum Blend
  publication-title: Mater. Chem. Phys.
  doi: 10.1016/j.matchemphys.2011.04.043
– volume: 139
  start-page: 621
  year: 2019
  ident: ref_13
  article-title: Chitosan-Alginate Beads as Encapsulating Agents for Yarrowia Lipolytica Lipase: Morphological, Physico-Chemical and Kinetic Characteristics
  publication-title: Int. J. Biol. Macromol.
  doi: 10.1016/j.ijbiomac.2019.08.009
– volume: 29
  start-page: 205
  year: 2012
  ident: ref_64
  article-title: Preparation, characterisation and viability of encapsulated Trichoderma harzianum UPM40 in alginate-montmorillonite clay
  publication-title: J. Microencapsul.
  doi: 10.3109/02652048.2012.659286
– volume: 55
  start-page: R1
  year: 1989
  ident: ref_177
  article-title: Nanocapsule Formation by Interfacial Polymer Deposition Following Solvent Displacement
  publication-title: Int. J. Pharm.
  doi: 10.1016/0378-5173(89)90281-0
– volume: 13
  start-page: 24
  year: 2017
  ident: ref_100
  article-title: Relation between Structure and Rheological/Thermal Properties of Agar. A Mini-Review on the Effect of Alkali Treatment and the Role of Agaropectin
  publication-title: Food Struct.
  doi: 10.1016/j.foostr.2016.10.003
– volume: 1
  start-page: 956
  year: 2011
  ident: ref_12
  article-title: Perspective of Recent Progress in Immobilization of Enzymes
  publication-title: ACS Catal.
  doi: 10.1021/cs200124a
– volume: 28
  start-page: 837
  year: 2002
  ident: ref_45
  article-title: Alginate in Drug Delivery Systems
  publication-title: Drug Dev. Ind. Pharm.
– volume: 124
  start-page: 336
  year: 2019
  ident: ref_87
  article-title: Emerging Contaminants of High Concern and Their Enzyme-Assisted Biodegradation–A Review
  publication-title: Environ. Int.
  doi: 10.1016/j.envint.2019.01.011
– volume: 90
  start-page: 66
  year: 2020
  ident: ref_20
  article-title: Parameters Necessary to Define an Immobilized Enzyme Preparation
  publication-title: Process. Biochem.
  doi: 10.1016/j.procbio.2019.11.026
– volume: 2015
  start-page: 145903
  year: 2015
  ident: ref_95
  article-title: Improvement of Starch Digestion Using α-Amylase Entrapped in Pectin-Polyvinyl Alcohol Blend
  publication-title: BioMed Res. Int.
  doi: 10.1155/2015/145903
– volume: 98
  start-page: 1191
  year: 2013
  ident: ref_90
  article-title: Co-Conjugation Vis-à-Vis Individual Conjugation of α-Amylase and Glucoamylase for Hydrolysis of Starch
  publication-title: Carbohydr. Polym.
  doi: 10.1016/j.carbpol.2013.07.032
– volume: 5
  start-page: 1112
  year: 2020
  ident: ref_17
  article-title: First-Generation Shaped Gel Reactors Based on Photo-Patterned Hybrid Hydrogels
  publication-title: React. Chem. Eng.
  doi: 10.1039/D0RE00109K
– volume: 1494
  start-page: 012028
  year: 2020
  ident: ref_58
  article-title: Improved Reuse and Affinity of Enzyme Using Immobilized Amylase on Alginate Matrix
  publication-title: J. Phys. Conf. Ser.
  doi: 10.1088/1742-6596/1494/1/012028
– volume: 68
  start-page: 53
  year: 2017
  ident: ref_179
  article-title: Electrospinning of Food Proteins and Polysaccharides
  publication-title: Food Hydrocoll.
  doi: 10.1016/j.foodhyd.2016.10.022
– volume: 67
  start-page: 85
  year: 2017
  ident: ref_79
  article-title: Lactase (β-Galactosidase) Encapsulation in Hydrogel Beads with Controlled Internal PH Microenvironments: Impact of Bead Characteristics on Enzyme Activity
  publication-title: Food Hydrocoll.
  doi: 10.1016/j.foodhyd.2017.01.005
– volume: 31
  start-page: 143
  year: 2004
  ident: ref_80
  article-title: Entrapment of Lipase into K-Carrageenan Beads and Its Use in Hydrolysis of Olive Oil in Biphasic System
  publication-title: J. Mol. Catalysis. B Enzym.
  doi: 10.1016/j.molcatb.2004.08.004
– volume: 1479
  start-page: 95
  year: 2017
  ident: ref_68
  article-title: Polymeric Materials for Perm-Selective Coating of Alginate Microbeads
  publication-title: Methods Mol. Biol.
  doi: 10.1007/978-1-4939-6364-5_7
– volume: 41
  start-page: 343
  year: 2006
  ident: ref_54
  article-title: Starch Hydrolysis by the Action of an Entrapped in Alginate Capsules α-Amylase from Bacillus Subtilis
  publication-title: Process. Biochem.
  doi: 10.1016/j.procbio.2005.01.028
– ident: ref_126
  doi: 10.1371/journal.pone.0047154
– volume: 169
  start-page: 289
  year: 2013
  ident: ref_140
  article-title: Surfactant Free Preparation of Biodegradable Dendritic Polyglycerol Nanogels by Inverse Nanoprecipitation for Encapsulation and Release of Pharmaceutical Biomacromolecules
  publication-title: J. Control. Release
  doi: 10.1016/j.jconrel.2012.12.008
– volume: 58
  start-page: 21
  year: 2016
  ident: ref_143
  article-title: Microencapsulation of Natural Antioxidants for Food Application—The Specific Case of Coffee Antioxidants—A Review
  publication-title: Trends Food Sci. Technol.
  doi: 10.1016/j.tifs.2016.10.012
– volume: 42
  start-page: 1681
  year: 2019
  ident: ref_93
  article-title: Alginate-Pectin Co-Encapsulation of Dextransucrase and Dextranase for Oligosaccharide Production from Sucrose Feedstocks
  publication-title: Bioprocess. Biosyst. Eng.
  doi: 10.1007/s00449-019-02164-z
– volume: 151
  start-page: 578
  year: 2008
  ident: ref_89
  article-title: Effects of Organic Solvents on Immobilized Lipase in Pectin Microspheres
  publication-title: Appl. Biochem. Biotechnol.
  doi: 10.1007/s12010-008-8233-0
– ident: ref_127
  doi: 10.1016/B978-0-12-819820-9.00024-7
– volume: 95
  start-page: 1994
  year: 2006
  ident: ref_50
  article-title: Physicochemical Characterization of Papain Entrapped in Ionotropically Cross-Linked Kappa-Carrageenan Gel Beads for Stability Improvement Using Doehlert Shell Design
  publication-title: J. Pharm. Sci.
  doi: 10.1002/jps.20665
SSID ssj0000456617
Score 2.432316
SecondaryResourceType review_article
Snippet Enzymes are versatile biomolecules with broad applications. Since they are biological molecules, they can be easily destabilized when placed in adverse...
SourceID unpaywall
pubmedcentral
proquest
crossref
SourceType Open Access Repository
Aggregation Database
Enrichment Source
Index Database
StartPage 4061
SubjectTerms Biocatalysts
Biocompatibility
Biomolecules
Biopolymers
Chitosan
Chymotrypsin
Encapsulation
Enzyme activity
Enzymes
Galactosidase
Lysozyme
Polyethylene
Polymerization
Polymers
Protective structures
Proteins
Review
Sodium alginate
Spray drying
Stability
Toxicity
SummonAdditionalLinks – databaseName: ProQuest Central
  dbid: BENPR
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV3dT9swED-x8sBeJmCb1g2mIE3byyxcx_now4Q6VoSQVqFpTLxF_gSk4HRrq6n89btLk0AnwWt8ia272Pc7--c7gA90mJQgjmfCJYZJpznLnbfMcY2TSUoZ12z375P09EKeXSaXGzBp78IQrbJdE-uF2laG9sgPEXfnGE8NE3k0_c2oahSdrrYlNFRTWsF-qVOMPYNNQZmxerD5dTw5_9HtuhCAQZ-9SraJX-OH06pc3mJIFpNnW3dO94jzf77k1iJM1fKvKssHzuhkG140KDIarcy-Axsu7MLWcVu87SWMzqlDhHaRmkXjYBQGw8R6C1fRiC5T4fNgo2-uJFrGMvrlrmt6XFR5lL7DN2ev4OJk_PP4lDXVEphBjDNniMySISnYJW5oDOdWKCmVyK1JfaYH3KY-lqlwPjcYVMReGZ1xneU6dS7jKn4NvVAF9wYihAE5dwPrpVdSOAy-vRBaC3RsFuGH78PnVk2FaVKJU0WLssCQgrRarGm1Dx878ekqh8ZjgnutzotmKs2Ke8P34aBrRnXSyYYKrlqsZBKKtVEmW7NV1yGl0V5vCTfXdTrtPE2GuJT14VNn1aeH-fbpYb6D54KIL4MBE_Ee9OZ_Fm4fkctcv29-x3-l6vH0
  priority: 102
  providerName: ProQuest
Title Polymers as Encapsulating Agents and Delivery Vehicles of Enzymes
URI https://www.proquest.com/docview/2608133954
https://www.proquest.com/docview/2608538374
https://pubmed.ncbi.nlm.nih.gov/PMC8659040
https://www.mdpi.com/2073-4360/13/23/4061/pdf?version=1637663901
UnpaywallVersion publishedVersion
Volume 13
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
journalDatabaseRights – providerCode: PRVFSB
  databaseName: Free Full-Text Journals in Chemistry
  customDbUrl:
  eissn: 2073-4360
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000456617
  issn: 2073-4360
  databaseCode: HH5
  dateStart: 20090101
  isFulltext: true
  titleUrlDefault: http://abc-chemistry.org/
  providerName: ABC ChemistRy
– providerCode: PRVAFT
  databaseName: Open Access Digital Library
  customDbUrl:
  eissn: 2073-4360
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000456617
  issn: 2073-4360
  databaseCode: KQ8
  dateStart: 20090101
  isFulltext: true
  titleUrlDefault: http://grweb.coalliance.org/oadl/oadl.html
  providerName: Colorado Alliance of Research Libraries
– providerCode: PRVEBS
  databaseName: Academic Search Ultimate - eBooks
  customDbUrl: https://search.ebscohost.com/login.aspx?authtype=ip,shib&custid=s3936755&profile=ehost&defaultdb=asn
  eissn: 2073-4360
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000456617
  issn: 2073-4360
  databaseCode: ABDBF
  dateStart: 20100901
  isFulltext: true
  titleUrlDefault: https://search.ebscohost.com/direct.asp?db=asn
  providerName: EBSCOhost
– providerCode: PRVEBS
  databaseName: EBSCOhost Food Science Source
  customDbUrl:
  eissn: 2073-4360
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0000456617
  issn: 2073-4360
  databaseCode: A8Z
  dateStart: 20100901
  isFulltext: true
  titleUrlDefault: https://search.ebscohost.com/login.aspx?authtype=ip,uid&profile=ehost&defaultdb=fsr
  providerName: EBSCOhost
– providerCode: PRVEBS
  databaseName: Inspec with Full Text
  customDbUrl:
  eissn: 2073-4360
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0000456617
  issn: 2073-4360
  databaseCode: ADMLS
  dateStart: 20100901
  isFulltext: true
  titleUrlDefault: https://www.ebsco.com/products/research-databases/inspec-full-text
  providerName: EBSCOhost
– providerCode: PRVFQY
  databaseName: GFMER Free Medical Journals
  customDbUrl:
  eissn: 2073-4360
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000456617
  issn: 2073-4360
  databaseCode: GX1
  dateStart: 20090101
  isFulltext: true
  titleUrlDefault: http://www.gfmer.ch/Medical_journals/Free_medical.php
  providerName: Geneva Foundation for Medical Education and Research
– providerCode: PRVHPJ
  databaseName: ROAD: Directory of Open Access Scholarly Resources
  customDbUrl:
  eissn: 2073-4360
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000456617
  issn: 2073-4360
  databaseCode: M~E
  dateStart: 20090101
  isFulltext: true
  titleUrlDefault: https://road.issn.org
  providerName: ISSN International Centre
– providerCode: PRVAQN
  databaseName: PubMed Central
  customDbUrl:
  eissn: 2073-4360
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000456617
  issn: 2073-4360
  databaseCode: RPM
  dateStart: 20160101
  isFulltext: true
  titleUrlDefault: https://www.ncbi.nlm.nih.gov/pmc/
  providerName: National Library of Medicine
– providerCode: PRVPQU
  databaseName: ProQuest Central
  customDbUrl: http://www.proquest.com/pqcentral?accountid=15518
  eissn: 2073-4360
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000456617
  issn: 2073-4360
  databaseCode: BENPR
  dateStart: 20090101
  isFulltext: true
  titleUrlDefault: https://www.proquest.com/central
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: ProQuest Technology Collection
  customDbUrl:
  eissn: 2073-4360
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000456617
  issn: 2073-4360
  databaseCode: 8FG
  dateStart: 20090101
  isFulltext: true
  titleUrlDefault: https://search.proquest.com/technologycollection1
  providerName: ProQuest
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3db9MwED9B-zBeYONDK2xVkBC84MWxnY8-obK1m5CoKkRReYpsx2YTwa1oC-r-es5NUtZJICQeE58TO3f2_X7x-Qzwwi8mxYjjCTOxJsIoSjJjC2KowsEkhOCbaPf3o-RiIt5N4-mNXfw-rBKp-NVmkmZofwSlaRjxkPHQO59wXtg3P-p_SQgmUnSZPb-Bq53EiMZb0J6Mxv3P_ky5pnaVWpOjWDifletvSMC4f9SuK_qNL29HR-6t3Fyuf8qyvOF6hg9ANo2uIk6-nqyW6kRf38rn-D-92of7NS4N-pUhHcAd4x7C3mlzHNwj6I99p7BuIBfBwGmJ9NrH0bkvQd9vz8L7rgjOTOkDPdbBJ3O5CbgLZhalr7Hm4jFMhoOPpxekPn-BaERNS4JYL-55lZnY9LSmtGBSCMmyQic2VREtEstFwozNNNIUbqVWKVVpphJjUir5E2i5mTOHECCwyKiJCiusFMwgnbeMKcXQVRYIaGwHXjeqyHWdnNyfkVHmSFK85vIdzXXg5VZ8XmXl-JPgUaPXvB6cixwpXIbUvBeLDjzfFuPn9Gsl0pnZqpKJPXtHmXTHHrYv9Im5d0vc1eUmQXeGpoiTYwdebS3n7818-s-Sz-Ae81E1UUQYP4LW8vvKHCMsWqou3M2G511ovx2Mxh_w6nwadevR8Asifg4d
linkProvider Unpaywall
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1Lb9NAEB6V9hAuCAqIQEuNxOPCqpv1-nWoUGhTpbSNKtSi3sw-aSV3HUiiKv1x_DZmHdslSPTWq3dsj2Yf8327szMAb_1hUoQ4njATKcKNpCQ1VhNDJU4mznlYRbsfj-LhGf9yHp2vwO_mLowPq2zWxGqh1qXye-TbiLtT5FNZxD-NfxJfNcqfrjYlNERdWkHvVCnG6osdh2Z-jRRusnOwh_39jrH9wenukNRVBohCbDAliGiizCtmIpMpRalmgnPBUq1im8ge1bENecyMTRWC8dAKJRMqk1TGxiRUhPjdB7DGQ54h-Vv7PBidfG13eTxgQoywSO6J2tPtcVnMr5ACht6TLjvDW4T7b3xmZ-bGYn4tiuIv57f_GB7VqDXoL4bZE1gxbh06u02xuKfQP_E_RCgZiEkwcEog-fZRdu5H0PeXt_C508GeKXwYyDz4Zi6qcLygtCh9g29OnsHZvdjtOay60pkXECDsSKnpacut4Mwg2beMScnQkWqEO7YLHxsz5apOXe4raBQ5Uhhv1XzJql1434qPFzk7_ie40dg8r6fuJL8daF140zajOf1JinCmnC1kIs_tUSZZ6qv2hz5t93KLu7yo0nencZTh0tmFD22v3q3my7vV3ILO8PT4KD86GB2-gofMB930eoSFG7A6_TUzm4iapvJ1PTQD-H7fs-EP7qEwoQ
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1LbxMxEB6VIlEuqLxEaIFF4nHBiuP1PnJAKGoaWgpVDxT1trW9NkVavClJVIWfxq_rzL5KkOit1_Xs7mg84_nGHs8AvKLDpAhxPBM2MkxazVlqXc4s12hMUsqwynb_chjvHctPJ9HJGvxp78JQWmW7JlYLdV4a2iPvI-5OMZ4aRrLvmrSIo_Hkw_ScUQcpOmlt22nUKnJglxcYvs3e749xrl8LMdn9urPHmg4DzCAumDNEM9GQmLKRHRrDeS6UlEqkuYldogc8j10oY2FdahCIh04ZnXCdpDq2NuEqxO_egtsJVXGnW-qTj93-DkElRAd1WU_km_enZbH8icFfSD501Q1eYdt_MzM3Fn6qlheqKP5ye5NNuNfg1WBUK9h9WLP-AWzstG3iHsLoiH6IIDJQs2DXG4VhN-XX-e_BiK5t4XOfB2NbUALIMvhmz6pEvKB0SP0b35w9guMbkdpjWPelt08gQMCRcjvInXRKCothvhNCa4EuNEeg43rwrhVTZpqi5dQ7o8gweCGpZitS7cGbjnxaV-v4H-F2K_OsMdpZdqViPXjZDaM46QxFeVsuapqIonqkSVbmqvshFexeHfE_zqrC3WkcDXHR7MHbblavZ_Pp9Wy-gDtoA9nn_cODLbgrKNtmMGAi3Ib1-a-FfYZwaa6fV3oZwOlNG8IltcYuOw
linkToUnpaywall http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3db9MwED-h7mG88LUhCgMFadpe5sWxnY8-oWpsmpCY9rBO4ymynfM2EdyKtqDur-fcJGWdBELiNT4nce7s-_3i8x3AbthMSgnHM4GpZQoNZwW6iiE3NJmUUnIZ7f75LDsdqU9X6dW9U_whrJKo-O1ykRZkf4ykeZzIWMg4OJ94UrkPP9p_SQQmcnKZg3CAayNLCY33YGN0dj78EmrKdb2b1JqSxOLJuF58IwImw63WXdFvfPkwOnJz7id68VPX9T3Xc_IUdPfSTcTJ18P5zBzauwf5HP9nVM_gSYtLo2FjSM_hEfoXsHnUlYPbguF5GBT1jfQ0OvZWE70OcXT-OhqG41l03VfRR6xDoMciusSbZcBdNHYkfUc9p9swOjm-ODplbf0FZgk1zRhhvXQQVIYpDqzlvBJaKS2KymYuNwmvMidVJtAVlmiKdNqanJu8MBlizrV8CT0_9vgKIgIWBcekcsppJZDovBPCGEGusiJA4_pw0KmitG1y8lAjoy6JpATNlWua68PeSnzSZOX4k-BOp9eynZzTkihcQdR8kKo-vF810-cMeyXa43jeyKSBvZNMvmYPqweGxNzrLf72ZpmguyBTpMWxD_sry_n7a77-Z8k38FiEqJokYULuQG_2fY5vCRbNzLvW8n8BMw4KrA
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=Polymers+as+Encapsulating+Agents+and+Delivery+Vehicles+of+Enzymes&rft.jtitle=Polymers&rft.au=da+S.+Pereira%2C+Adejanildo&rft.au=Souza%2C+Camila+P.+L.&rft.au=Moraes%2C+Lidiane&rft.au=Fontes-Sant%E2%80%99Ana%2C+Gizele+C.&rft.date=2021-11-23&rft.pub=MDPI&rft.eissn=2073-4360&rft.volume=13&rft.issue=23&rft_id=info:doi/10.3390%2Fpolym13234061&rft_id=info%3Apmid%2F34883565&rft.externalDocID=PMC8659040
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2073-4360&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2073-4360&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2073-4360&client=summon