Functional characterization of a bacterial expansin from Bacillus subtilis for enhanced enzymatic hydrolysis of cellulose
Expansin is a plant protein family that induces plant cell wall-loosening and cellulose disruption without exerting cellulose-hydrolytic activity. Expansin-like proteins have also been found in other eukaryotes such as nematodes and fungi. While searching for an expansin produced by bacteria, we fou...
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| Published in | Biotechnology and bioengineering Vol. 102; no. 5; pp. 1342 - 1353 |
|---|---|
| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Hoboken
Wiley Subscription Services, Inc., A Wiley Company
01.04.2009
Wiley Wiley Subscription Services, Inc |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0006-3592 1097-0290 1097-0290 |
| DOI | 10.1002/bit.22193 |
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| Abstract | Expansin is a plant protein family that induces plant cell wall-loosening and cellulose disruption without exerting cellulose-hydrolytic activity. Expansin-like proteins have also been found in other eukaryotes such as nematodes and fungi. While searching for an expansin produced by bacteria, we found that the BsEXLX1 protein from Bacillus subtilis had a structure that was similar to that of a β-expansin produced by maize. Therefore, we cloned the BsEXLX1 gene and expressed it in Escherichia coli to evaluate its function. When incubated with filter paper as a cellulose substrate, the recombinant protein exhibited both cellulose-binding and cellulose-weakening activities, which are known functions of plant expansins. In addition, evaluation of the enzymatic hydrolysis of filter paper revealed that the recombinant protein also displayed a significant synergism when mixed with cellulase. By comparing the activity of a mixture of cellulase and the bacterial expansin to the additive activity of the individual proteins, the synergistic activity was found to be as high as 240% when filter paper was incubated with cellulase and BsEXLX1, which was 5.7-fold greater than the activity of cellulase alone. However, this synergistic effect was observed when only a low dosage of cellulase was used. This is the first study to characterize the function of an expansin produced by a non-eukaryotic source. Biotechnol. Bioeng. 2009;102: 1342-1353. |
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| AbstractList | Expansin is a plant protein family that induces plant cell wall-loosening and cellulose disruption without exerting cellulose-hydrolytic activity. Expansin-like proteins have also been found in other eukaryotes such as nematodes and fungi. While searching for an expansin produced by bacteria, we found that the BsEXLX1 protein from Bacillus subtilis had a structure that was similar to that of a β-expansin produced by maize. Therefore, we cloned the BsEXLX1 gene and expressed it in Escherichia coli to evaluate its function. When incubated with filter paper as a cellulose substrate, the recombinant protein exhibited both cellulose-binding and cellulose-weakening activities, which are known functions of plant expansins. In addition, evaluation of the enzymatic hydrolysis of filter paper revealed that the recombinant protein also displayed a significant synergism when mixed with cellulase. By comparing the activity of a mixture of cellulase and the bacterial expansin to the additive activity of the individual proteins, the synergistic activity was found to be as high as 240% when filter paper was incubated with cellulase and BsEXLX1, which was 5.7-fold greater than the activity of cellulase alone. However, this synergistic effect was observed when only a low dosage of cellulase was used. This is the first study to characterize the function of an expansin produced by a non-eukaryotic source. Biotechnol. Bioeng. 2009;102: 1342-1353. Expansin is a plant protein family that induces plant cell wall-loosening and cellulose disruption without exerting cellulose-hydrolytic activity. Expansin-like proteins have also been found in other eukaryotes such as nematodes and fungi. While searching for an expansin produced by bacteria, we found that the BsEXLX1 protein from Bacillus subtilis had a structure that was similar to that of a -expansin produced by maize. Therefore, we cloned the BsEXLX1 gene and expressed it in Escherichia coli to evaluate its function. When incubated with filter paper as a cellulose substrate, the recombinant protein exhibited both cellulose-binding and cellulose-weakening activities, which are known functions of plant expansins. In addition, evaluation of the enzymatic hydrolysis of filter paper revealed that the recombinant protein also displayed a significant synergism when mixed with cellulase. By comparing the activity of a mixture of cellulase and the bacterial expansin to the additive activity of the individual proteins, the synergistic activity was found to be as high as 240% when filter paper was incubated with cellulase and BsEXLX1, which was 5.7-fold greater than the activity of cellulase alone. However, this synergistic effect was observed when only a low dosage of cellulase was used. This is the first study to characterize the function of an expansin produced by a non-eukaryotic source. Biotechnol. Bioeng. 2009; 102: 1342-1353. Expansin is a plant protein family that induces plant cell wall-loosening and cellulose disruption without exerting cellulose-hydrolytic activity. Expansin-like proteins have also been found in other eukaryotes such as nematodes and fungi. While searching for an expansin produced by bacteria, we found that the BsEXLX1 protein from Bacillus subtilis had a structure that was similar to that of a beta-expansin produced by maize. Therefore, we cloned the BsEXLX1 gene and expressed it in Escherichia coli to evaluate its function. When incubated with filter paper as a cellulose substrate, the recombinant protein exhibited both cellulose-binding and cellulose-weakening activities, which are known functions of plant expansins. In addition, evaluation of the enzymatic hydrolysis of filter paper revealed that the recombinant protein also displayed a significant synergism when mixed with cellulase. By comparing the activity of a mixture of cellulase and the bacterial expansin to the additive activity of the individual proteins, the synergistic activity was found to be as high as 240% when filter paper was incubated with cellulase and BsEXLX1, which was 5.7-fold greater than the activity of cellulase alone. However, this synergistic effect was observed when only a low dosage of cellulase was used. This is the first study to characterize the function of an expansin produced by a non-eukaryotic source. Expansin is a plant protein family that induces plant cell wall-loosening and cellulose disruption without exerting cellulose-hydrolytic activity. Expansin-like proteins have also been found in other eukaryotes such as nematodes and fungi. While searching for an expansin produced by bacteria, we found that the BsEXLX1 protein from Bacillus subtilis had a structure that was similar to that of a β-expansin produced by maize. Therefore, we cloned the BsEXLX1 gene and expressed it in Escherichia coli to evaluate its function. When incubated with filter paper as a cellulose substrate, the recombinant protein exhibited both cellulose-binding and cellulose-weakening activities, which are known functions of plant expansins. In addition, evaluation of the enzymatic hydrolysis of filter paper revealed that the recombinant protein also displayed a significant synergism when mixed with cellulase. By comparing the activity of a mixture of cellulase and the bacterial expansin to the additive activity of the individual proteins, the synergistic activity was found to be as high as 240% when filter paper was incubated with cellulase and BsEXLX1, which was 5.7-fold greater than the activity of cellulase alone. However, this synergistic effect was observed when only a low dosage of cellulase was used. This is the first study to characterize the function of an expansin produced by a non-eukaryotic source. [PUBLICATION ABSTRACT] Expansin is a plant protein family that induces plant cell wall‐loosening and cellulose disruption without exerting cellulose‐hydrolytic activity. Expansin‐like proteins have also been found in other eukaryotes such as nematodes and fungi. While searching for an expansin produced by bacteria, we found that the BsEXLX1 protein from Bacillus subtilis had a structure that was similar to that of a β‐expansin produced by maize. Therefore, we cloned the BsEXLX1 gene and expressed it in Escherichia coli to evaluate its function. When incubated with filter paper as a cellulose substrate, the recombinant protein exhibited both cellulose‐binding and cellulose‐weakening activities, which are known functions of plant expansins. In addition, evaluation of the enzymatic hydrolysis of filter paper revealed that the recombinant protein also displayed a significant synergism when mixed with cellulase. By comparing the activity of a mixture of cellulase and the bacterial expansin to the additive activity of the individual proteins, the synergistic activity was found to be as high as 240% when filter paper was incubated with cellulase and BsEXLX1, which was 5.7‐fold greater than the activity of cellulase alone. However, this synergistic effect was observed when only a low dosage of cellulase was used. This is the first study to characterize the function of an expansin produced by a non‐eukaryotic source. Biotechnol. Bioeng. 2009;102: 1342–1353. © 2008 Wiley Periodicals, Inc. Expansin is a plant protein family that induces plant cell wall-loosening and cellulose disruption without exerting cellulose-hydrolytic activity. Expansin-like proteins have also been found in other eukaryotes such as nematodes and fungi. While searching for an expansin produced by bacteria, we found that the BsEXLX1 protein from Bacillus subtilis had a structure that was similar to that of a beta-expansin produced by maize. Therefore, we cloned the BsEXLX1 gene and expressed it in Escherichia coli to evaluate its function. When incubated with filter paper as a cellulose substrate, the recombinant protein exhibited both cellulose-binding and cellulose-weakening activities, which are known functions of plant expansins. In addition, evaluation of the enzymatic hydrolysis of filter paper revealed that the recombinant protein also displayed a significant synergism when mixed with cellulase. By comparing the activity of a mixture of cellulase and the bacterial expansin to the additive activity of the individual proteins, the synergistic activity was found to be as high as 240% when filter paper was incubated with cellulase and BsEXLX1, which was 5.7-fold greater than the activity of cellulase alone. However, this synergistic effect was observed when only a low dosage of cellulase was used. This is the first study to characterize the function of an expansin produced by a non-eukaryotic source.Expansin is a plant protein family that induces plant cell wall-loosening and cellulose disruption without exerting cellulose-hydrolytic activity. Expansin-like proteins have also been found in other eukaryotes such as nematodes and fungi. While searching for an expansin produced by bacteria, we found that the BsEXLX1 protein from Bacillus subtilis had a structure that was similar to that of a beta-expansin produced by maize. Therefore, we cloned the BsEXLX1 gene and expressed it in Escherichia coli to evaluate its function. When incubated with filter paper as a cellulose substrate, the recombinant protein exhibited both cellulose-binding and cellulose-weakening activities, which are known functions of plant expansins. In addition, evaluation of the enzymatic hydrolysis of filter paper revealed that the recombinant protein also displayed a significant synergism when mixed with cellulase. By comparing the activity of a mixture of cellulase and the bacterial expansin to the additive activity of the individual proteins, the synergistic activity was found to be as high as 240% when filter paper was incubated with cellulase and BsEXLX1, which was 5.7-fold greater than the activity of cellulase alone. However, this synergistic effect was observed when only a low dosage of cellulase was used. This is the first study to characterize the function of an expansin produced by a non-eukaryotic source. Expansin is a plant protein family that induces plant cell wall‐loosening and cellulose disruption without exerting cellulose‐hydrolytic activity. Expansin‐like proteins have also been found in other eukaryotes such as nematodes and fungi. While searching for an expansin produced by bacteria, we found that the BsEXLX1 protein from Bacillus subtilis had a structure that was similar to that of a β‐expansin produced by maize. Therefore, we cloned the BsEXLX1 gene and expressed it in Escherichia coli to evaluate its function. When incubated with filter paper as a cellulose substrate, the recombinant protein exhibited both cellulose‐binding and cellulose‐weakening activities, which are known functions of plant expansins. In addition, evaluation of the enzymatic hydrolysis of filter paper revealed that the recombinant protein also displayed a significant synergism when mixed with cellulase. By comparing the activity of a mixture of cellulase and the bacterial expansin to the additive activity of the individual proteins, the synergistic activity was found to be as high as 240% when filter paper was incubated with cellulase and BsEXLX1, which was 5.7‐fold greater than the activity of cellulase alone. However, this synergistic effect was observed when only a low dosage of cellulase was used. This is the first study to characterize the function of an expansin produced by a non‐eukaryotic source. Biotechnol. Bioeng. 2009;102: 1342–1353. © 2008 Wiley Periodicals, Inc. |
| Author | Kim, Eun Sil Kim, Kyoung Heon Lee, Hee Jin Bang, Won-Gi Choi, In-Geol |
| Author_xml | – sequence: 1 fullname: Kim, Eun Sil – sequence: 2 fullname: Lee, Hee Jin – sequence: 3 fullname: Bang, Won-Gi – sequence: 4 fullname: Choi, In-Geol – sequence: 5 fullname: Kim, Kyoung Heon |
| BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21228067$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/19058186$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1007/BF02920125 10.1016/S1369-5266(99)00039-4 10.1002/bit.260420811 10.1073/pnas.0605979103 10.1002/bit.20942 10.1073/pnas.91.14.6574 10.1038/427030a 10.1038/nbt0208-169 10.1016/S0960-8524(97)00103-X 10.1002/jcc.20084 10.1038/35030000 10.1042/bj2550895 10.1007/10_2007_066 10.1002/bit.21856 10.1093/nar/18.20.6069 10.1002/bit.21636 10.1002/bit.20286 10.1186/gb-2005-6-12-242 10.1016/j.enzmictec.2007.05.012 10.1007/s11103-004-0158-6 10.1021/bp0340180 10.1038/nmeth.f.202 10.1002/bit.260440907 10.1002/bit.20783 10.1016/0960-8524(91)90120-9 10.1021/ie50421a003 10.1074/jbc.M209554200 10.1046/j.1432-1033.2002.03095.x 10.2210/pdb2bh0/pdb 10.1385/ABAB:84-86:1-9:217 10.1093/bioinformatics/16.6.566 10.1016/j.biortech.2004.10.017 10.1073/pnas.160216697 |
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| Issue | 5 |
| Keywords | Enzyme Bacillus subtilis Cellulose cellulose hydrolysis bacterial expansin Biofuel Bacillaceae Synergism Glycosylases Characterization Hydrolysis structural homolog Bacillales Cellulase Glycosidases Hydrolases Bacteria |
| Language | English |
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| References | Berlin A, Maximenko V, Bura R, Kang KY, Gilkes N, Saddler J. 2006. A rapid microassay to evaluate enzymatic hydrolysis of lignocellulosic substrates. Biotechnol Bioeng 93(5): 880-886. Woodward J, Lima M, Lee NE. 1988. The role of cellulase concentration in determining the degree of synergism in the hydrolysis of microcrystalline cellulose. Biochem J 255(3): 895-899. Saloheimo M, Paloheimo M, Hakola S, Pere J, Swanson B, Nyyssonen E, Bhatia A, Ward M, Penttila M. 2002. Swollenin, a Trichoderma reesei protein with sequence similarity to the plant expansins, exhibits disruption activity on cellulosic materials. Eur J Biochem 269(17): 4202-4211. Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. 2004. UCSF Chimera-A visualization system for exploratory research and analysis. J Comput Chem 25(13): 1605-1612. Gregg DJ, Boussaid A, Saddler JN. 1998. Techno-economic evaluations of a generic wood-to-ethanol process: Effect of increased cellulose yields and enzyme recycle. Bioresource Technol 63(1): 7-12. Xiao ZZ, Storms R, Tsang A. 2004. Microplate-based filter paper assay to measure total cellulase activity. Biotechnol Bioeng 88(7): 832-837. Boraston AB, Kwan E, Chiu P, Warren RAJ, Kilburn DG. 2003. Recognition and hydrolysis of noncrystalline cellulose. J Biol Chem 278(8): 6120-6127. Qin L, Kudla U, Roze EHA, Goverse A, Popeijus H, Nieuwland J, Overmars H, Jones JT, Schots A, Smant G, et al. 2004. Plant degradation: A nematode expansin acting on plants. Nature 427(6969): 30-30. Yang B, Willies DM, Wyman CE. 2006. Changes in the enzymatic hydrolysis rate of Avicel cellulose with conversion. Biotechnol Bioeng 94(6): 1122-1128. Han YJ, Chen HZ. 2007. Synergism between corn stover protein and cellulase. Enzyme Microb Technol 41(5): 638-645. Irwin DC, Spezio M, Walker LP, Wilson DB. 1993. Activity studies of eight purified cellulases-Specificity, synergism, and binding domain effects. Biotechnol Bioeng 42(8): 1002-1013. Kende H, Bradford KJ, Brummell DA, Cho HT, Cosgrove DJ, Fleming AJ, Gehring C, Lee Y, McQueen-Mason S, Rose JKC, et al. 2004. Nomenclature for members of the expansin superfamily of genes and proteins. Plant Mol Biol 55(3): 311-314. Cosgrove DJ. 2000a. Loosening of plant cell walls by expansins. Nature 407(6802): 321-326. Sherrad EC, Kressman FW. 1945. Review of processes in the United States prior to World War II. Ind Eng Chem 37(1): 5-8. Nguyen QA, Tucker MP, Boynton BL, Keller FA, Schell DJ. 1998. Dilute acid pretreatment of softwoods. Appl Biochem Biotechnol 70-72: 77-87. Yennawar NH, Li LC, Dudzinski DM, Tabuchi A, Cosgrove DJ. 2006. Crystal structure and activities of EXPB1 (Zea m 1), a β-expansin and group-1 pollen allergen from maize. Proc Natl Acad Sci USA 103(40): 14664-14671. Adney B, Baker J. 1996. Measurement of cellulase activities, Chemical Analysis and Testing Task: LAP-006. Golden, CO, USA: National Renewable Energy Laboratory. Aslanidis C, Dejong PJ. 1990. Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res 18(20): 6069-6074. Moser F, Irwin D, Chen S, Wilson DB. 2008. Regulation and characterization of Thermobifida fusca carbohydrate-binding module proteins E7 and E8. Biotechnol Bioeng 100(6): 1066-1077. Graslund S, Nordlund P, Weigelt J, Bray J, Gileadi O, Knapp S, Oppermann U, Arrowsmith C, Hui R, Ming J, et al. 2008. Protein production and purification. Nat Methods 5: 135-146. Lynd LR, Laser MS, Bransby D, Dale BE, Davision B, Hamilton R, Himmel M, Keller H, McMillan JM, Sheehan J, et al. 2008. How biotech can transform biofuels. Nat Biotechnol 26(2): 169-172. Carrard G, Koivula A, Soderlund H, Beguin P. 2000. Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose. Proc Natl Acad Sci USA 97(19): 10342-10347. Sampedro J, Cosgrove DJ. 2005. The expansin superfamily. Genome Biol 6(12): 242-252. Rudolf A, Baudel H, Zacchi G, Hahn-Hagerdal B, Liden G. 2008. Simultaneous saccharification and fermentation of steam-pretreated bagasse using Saccharomyces cerevisiae TMB3400 and Pichia stipitis CBS6054. Biotechnol Bioeng 99: 783-790. Cosgrove DJ. 2000b. New genes and new biological roles for expansins. Curr Opin Plant Biol 3(1): 73-78. Kim KH, Tucker M, Nguyen Q. 2005. Conversion of bark-rich biomass mixture into fermentable sugar by two-stage dilute acid-catalyzed hydrolysis. Bioresource Technol 96(11): 1249-1255. Medve J, Stahlberg J, Tjerneld F. 1994. Adsorption and synergism of cellobiohydrolase-I and cellohydrolase-II of Trichoderma-reesei during hydrolysis of microcrystalline cellulose. Biotechnol Bioeng 44(9): 1064-1073. Baker JO, King MR, Adney WS, Decker SR, Vinzant TB, Lantz SE, Nieves RE, Thomas SR, Li LC, Cosgrove DJ, Himmel E. 2000. Investigation of the cell-wall loosening protein expansin as a possible additive in the enzymatic saccharification of lignocellulosic biomass. Appl Biochem Biotechnol 84-86: 217-223. McQueen-Mason S, Cosgrove DJ. 1994. Disruption of hydrogen-bonding between plant-cell wall polymers by proteins that wall extension. Proc Natl Acad Sci USA 91(14): 6574-6578. Wingren A, Galbe M, Zacchi G. 2003. Techno-economic evaluation of producing ethanol from softwood: Comparison of SSF and SHF and identification of bottlenecks. Biotechnol Prog 19(4): 1109-1117. Merino ST, Cherry J. 2007. Progress and challenges in enzyme development for biomass utilization. Adv Biochem Eng Biotechnol 108: 95-120. Holm L, Park J. 2000. DaliLite workbench for protein structure comparison. Bioinformatics 16(6): 566-567. Torget R, Himmel ME, Grohmann K. 1991. Dilute sulfuric acid pretreatment of hardwood bark. Bioresource Technol 35(3): 239-246. 2006; 93 2004; 88 2007; 108 2006; 94 1991; 35 2000b; 3 1990; 18 2004; 25 1945; 37 1993; 42 1994; 44 1996 2007 2006 2008; 5 2008; 99 2003; 19 1998; 63 2008; 100 2004; 427 2003; 278 2004; 55 2000; 16 2001 2000; 97 2005; 96 2008; 26 2002; 269 1988; 255 2005; 6 2000a; 407 2007; 41 1998; 70–72 1994; 91 2006; 103 2000; 84–86 Adney B (e_1_2_1_2_1) 1996 e_1_2_1_20_1 e_1_2_1_23_1 e_1_2_1_24_1 e_1_2_1_21_1 e_1_2_1_22_1 e_1_2_1_27_1 e_1_2_1_28_1 e_1_2_1_25_1 e_1_2_1_26_1 e_1_2_1_29_1 e_1_2_1_7_1 e_1_2_1_31_1 e_1_2_1_8_1 e_1_2_1_30_1 e_1_2_1_5_1 e_1_2_1_6_1 e_1_2_1_3_1 e_1_2_1_12_1 e_1_2_1_35_1 e_1_2_1_4_1 e_1_2_1_13_1 e_1_2_1_34_1 e_1_2_1_10_1 e_1_2_1_33_1 e_1_2_1_11_1 e_1_2_1_32_1 e_1_2_1_16_1 e_1_2_1_17_1 e_1_2_1_14_1 e_1_2_1_37_1 e_1_2_1_15_1 e_1_2_1_36_1 e_1_2_1_9_1 e_1_2_1_18_1 e_1_2_1_19_1 |
| References_xml | – reference: Saloheimo M, Paloheimo M, Hakola S, Pere J, Swanson B, Nyyssonen E, Bhatia A, Ward M, Penttila M. 2002. Swollenin, a Trichoderma reesei protein with sequence similarity to the plant expansins, exhibits disruption activity on cellulosic materials. Eur J Biochem 269(17): 4202-4211. – reference: Kende H, Bradford KJ, Brummell DA, Cho HT, Cosgrove DJ, Fleming AJ, Gehring C, Lee Y, McQueen-Mason S, Rose JKC, et al. 2004. Nomenclature for members of the expansin superfamily of genes and proteins. Plant Mol Biol 55(3): 311-314. – reference: Nguyen QA, Tucker MP, Boynton BL, Keller FA, Schell DJ. 1998. Dilute acid pretreatment of softwoods. Appl Biochem Biotechnol 70-72: 77-87. – reference: Torget R, Himmel ME, Grohmann K. 1991. Dilute sulfuric acid pretreatment of hardwood bark. Bioresource Technol 35(3): 239-246. – reference: Baker JO, King MR, Adney WS, Decker SR, Vinzant TB, Lantz SE, Nieves RE, Thomas SR, Li LC, Cosgrove DJ, Himmel E. 2000. Investigation of the cell-wall loosening protein expansin as a possible additive in the enzymatic saccharification of lignocellulosic biomass. Appl Biochem Biotechnol 84-86: 217-223. – reference: Adney B, Baker J. 1996. Measurement of cellulase activities, Chemical Analysis and Testing Task: LAP-006. Golden, CO, USA: National Renewable Energy Laboratory. – reference: Sampedro J, Cosgrove DJ. 2005. The expansin superfamily. Genome Biol 6(12): 242-252. – reference: Han YJ, Chen HZ. 2007. Synergism between corn stover protein and cellulase. Enzyme Microb Technol 41(5): 638-645. – reference: Sherrad EC, Kressman FW. 1945. Review of processes in the United States prior to World War II. Ind Eng Chem 37(1): 5-8. – reference: Cosgrove DJ. 2000a. Loosening of plant cell walls by expansins. Nature 407(6802): 321-326. – reference: Moser F, Irwin D, Chen S, Wilson DB. 2008. Regulation and characterization of Thermobifida fusca carbohydrate-binding module proteins E7 and E8. Biotechnol Bioeng 100(6): 1066-1077. – reference: Gregg DJ, Boussaid A, Saddler JN. 1998. Techno-economic evaluations of a generic wood-to-ethanol process: Effect of increased cellulose yields and enzyme recycle. Bioresource Technol 63(1): 7-12. – reference: Medve J, Stahlberg J, Tjerneld F. 1994. Adsorption and synergism of cellobiohydrolase-I and cellohydrolase-II of Trichoderma-reesei during hydrolysis of microcrystalline cellulose. Biotechnol Bioeng 44(9): 1064-1073. – reference: Yang B, Willies DM, Wyman CE. 2006. Changes in the enzymatic hydrolysis rate of Avicel cellulose with conversion. Biotechnol Bioeng 94(6): 1122-1128. – reference: Graslund S, Nordlund P, Weigelt J, Bray J, Gileadi O, Knapp S, Oppermann U, Arrowsmith C, Hui R, Ming J, et al. 2008. Protein production and purification. Nat Methods 5: 135-146. – reference: McQueen-Mason S, Cosgrove DJ. 1994. Disruption of hydrogen-bonding between plant-cell wall polymers by proteins that wall extension. Proc Natl Acad Sci USA 91(14): 6574-6578. – reference: Cosgrove DJ. 2000b. New genes and new biological roles for expansins. Curr Opin Plant Biol 3(1): 73-78. – reference: Wingren A, Galbe M, Zacchi G. 2003. Techno-economic evaluation of producing ethanol from softwood: Comparison of SSF and SHF and identification of bottlenecks. Biotechnol Prog 19(4): 1109-1117. – reference: Yennawar NH, Li LC, Dudzinski DM, Tabuchi A, Cosgrove DJ. 2006. Crystal structure and activities of EXPB1 (Zea m 1), a β-expansin and group-1 pollen allergen from maize. Proc Natl Acad Sci USA 103(40): 14664-14671. – reference: Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. 2004. UCSF Chimera-A visualization system for exploratory research and analysis. J Comput Chem 25(13): 1605-1612. – reference: Aslanidis C, Dejong PJ. 1990. Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res 18(20): 6069-6074. – reference: Boraston AB, Kwan E, Chiu P, Warren RAJ, Kilburn DG. 2003. Recognition and hydrolysis of noncrystalline cellulose. J Biol Chem 278(8): 6120-6127. – reference: Rudolf A, Baudel H, Zacchi G, Hahn-Hagerdal B, Liden G. 2008. Simultaneous saccharification and fermentation of steam-pretreated bagasse using Saccharomyces cerevisiae TMB3400 and Pichia stipitis CBS6054. Biotechnol Bioeng 99: 783-790. – reference: Carrard G, Koivula A, Soderlund H, Beguin P. 2000. Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose. Proc Natl Acad Sci USA 97(19): 10342-10347. – reference: Merino ST, Cherry J. 2007. Progress and challenges in enzyme development for biomass utilization. Adv Biochem Eng Biotechnol 108: 95-120. – reference: Qin L, Kudla U, Roze EHA, Goverse A, Popeijus H, Nieuwland J, Overmars H, Jones JT, Schots A, Smant G, et al. 2004. Plant degradation: A nematode expansin acting on plants. Nature 427(6969): 30-30. – reference: Xiao ZZ, Storms R, Tsang A. 2004. Microplate-based filter paper assay to measure total cellulase activity. Biotechnol Bioeng 88(7): 832-837. – reference: Lynd LR, Laser MS, Bransby D, Dale BE, Davision B, Hamilton R, Himmel M, Keller H, McMillan JM, Sheehan J, et al. 2008. How biotech can transform biofuels. Nat Biotechnol 26(2): 169-172. – reference: Irwin DC, Spezio M, Walker LP, Wilson DB. 1993. Activity studies of eight purified cellulases-Specificity, synergism, and binding domain effects. Biotechnol Bioeng 42(8): 1002-1013. – reference: Berlin A, Maximenko V, Bura R, Kang KY, Gilkes N, Saddler J. 2006. A rapid microassay to evaluate enzymatic hydrolysis of lignocellulosic substrates. Biotechnol Bioeng 93(5): 880-886. – reference: Kim KH, Tucker M, Nguyen Q. 2005. Conversion of bark-rich biomass mixture into fermentable sugar by two-stage dilute acid-catalyzed hydrolysis. Bioresource Technol 96(11): 1249-1255. – reference: Holm L, Park J. 2000. DaliLite workbench for protein structure comparison. Bioinformatics 16(6): 566-567. – reference: Woodward J, Lima M, Lee NE. 1988. The role of cellulase concentration in determining the degree of synergism in the hydrolysis of microcrystalline cellulose. Biochem J 255(3): 895-899. – volume: 100 start-page: 1066 issue: 6 year: 2008 end-page: 1077 article-title: Regulation and characterization of carbohydrate‐binding module proteins E7 and E8 publication-title: Biotechnol Bioeng – volume: 6 start-page: 242 issue: 12 year: 2005 end-page: 252 article-title: The expansin superfamily publication-title: Genome Biol – volume: 103 start-page: 14664 issue: 40 year: 2006 end-page: 14671 article-title: Crystal structure and activities of EXPB1 (Zea m 1), a β‐expansin and group‐1 pollen allergen from maize publication-title: Proc Natl Acad Sci USA – volume: 55 start-page: 311 issue: 3 year: 2004 end-page: 314 article-title: Nomenclature for members of the expansin superfamily of genes and proteins publication-title: Plant Mol Biol – volume: 26 start-page: 169 issue: 2 year: 2008 end-page: 172 article-title: How biotech can transform biofuels publication-title: Nat Biotechnol – volume: 70–72 start-page: 77 year: 1998 end-page: 87 article-title: Dilute acid pretreatment of softwoods publication-title: Appl Biochem Biotechnol – volume: 19 start-page: 1109 issue: 4 year: 2003 end-page: 1117 article-title: Techno‐economic evaluation of producing ethanol from softwood: Comparison of SSF and SHF and identification of bottlenecks publication-title: Biotechnol Prog – year: 2001 – year: 2007 – volume: 278 start-page: 6120 issue: 8 year: 2003 end-page: 6127 article-title: Recognition and hydrolysis of noncrystalline cellulose publication-title: J Biol Chem – year: 1996 – volume: 91 start-page: 6574 issue: 14 year: 1994 end-page: 6578 article-title: Disruption of hydrogen‐bonding between plant‐cell wall polymers by proteins that wall extension publication-title: Proc Natl Acad Sci USA – volume: 427 start-page: 30 issue: 6969 year: 2004 end-page: 30 article-title: Plant degradation: A nematode expansin acting on plants publication-title: Nature – volume: 97 start-page: 10342 issue: 19 year: 2000 end-page: 10347 article-title: Cellulose‐binding domains promote hydrolysis of different sites on crystalline cellulose publication-title: Proc Natl Acad Sci USA – volume: 88 start-page: 832 issue: 7 year: 2004 end-page: 837 article-title: Microplate‐based filter paper assay to measure total cellulase activity publication-title: Biotechnol Bioeng – volume: 108 start-page: 95 year: 2007 end-page: 120 article-title: Progress and challenges in enzyme development for biomass utilization publication-title: Adv Biochem Eng Biotechnol – volume: 407 start-page: 321 issue: 6802 year: 2000a end-page: 326 article-title: Loosening of plant cell walls by expansins publication-title: Nature – volume: 42 start-page: 1002 issue: 8 year: 1993 end-page: 1013 article-title: Activity studies of eight purified cellulases—Specificity, synergism, and binding domain effects publication-title: Biotechnol Bioeng – volume: 93 start-page: 880 issue: 5 year: 2006 end-page: 886 article-title: A rapid microassay to evaluate enzymatic hydrolysis of lignocellulosic substrates publication-title: Biotechnol Bioeng – volume: 3 start-page: 73 issue: 1 year: 2000b end-page: 78 article-title: New genes and new biological roles for expansins publication-title: Curr Opin Plant Biol – volume: 18 start-page: 6069 issue: 20 year: 1990 end-page: 6074 article-title: Ligation‐independent cloning of PCR products (LIC‐PCR) publication-title: Nucleic Acids Res – volume: 269 start-page: 4202 issue: 17 year: 2002 end-page: 4211 article-title: Swollenin, a protein with sequence similarity to the plant expansins, exhibits disruption activity on cellulosic materials publication-title: Eur J Biochem – volume: 94 start-page: 1122 issue: 6 year: 2006 end-page: 1128 article-title: Changes in the enzymatic hydrolysis rate of Avicel cellulose with conversion publication-title: Biotechnol Bioeng – volume: 37 start-page: 5 issue: 1 year: 1945 end-page: 8 article-title: Review of processes in the United States prior to World War II publication-title: Ind Eng Chem – volume: 25 start-page: 1605 issue: 13 year: 2004 end-page: 1612 article-title: UCSF Chimera—A visualization system for exploratory research and analysis publication-title: J Comput Chem – volume: 41 start-page: 638 issue: 5 year: 2007 end-page: 645 article-title: Synergism between corn stover protein and cellulase publication-title: Enzyme Microb Technol – volume: 84–86 start-page: 217 year: 2000 end-page: 223 article-title: Investigation of the cell‐wall loosening protein expansin as a possible additive in the enzymatic saccharification of lignocellulosic biomass publication-title: Appl Biochem Biotechnol – volume: 255 start-page: 895 issue: 3 year: 1988 end-page: 899 article-title: The role of cellulase concentration in determining the degree of synergism in the hydrolysis of microcrystalline cellulose publication-title: Biochem J – volume: 63 start-page: 7 issue: 1 year: 1998 end-page: 12 article-title: Techno‐economic evaluations of a generic wood‐to‐ethanol process: Effect of increased cellulose yields and enzyme recycle publication-title: Bioresource Technol – year: 2006 – volume: 5 start-page: 135 year: 2008 end-page: 146 article-title: Protein production and purification publication-title: Nat Methods – volume: 96 start-page: 1249 issue: 11 year: 2005 end-page: 1255 article-title: Conversion of bark‐rich biomass mixture into fermentable sugar by two‐stage dilute acid‐catalyzed hydrolysis publication-title: Bioresource Technol – volume: 35 start-page: 239 issue: 3 year: 1991 end-page: 246 article-title: Dilute sulfuric acid pretreatment of hardwood bark publication-title: Bioresource Technol – volume: 99 start-page: 783 year: 2008 end-page: 790 article-title: Simultaneous saccharification and fermentation of steam‐pretreated bagasse using TMB3400 and CBS6054 publication-title: Biotechnol Bioeng – volume: 44 start-page: 1064 issue: 9 year: 1994 end-page: 1073 article-title: Adsorption and synergism of cellobiohydrolase‐I and cellohydrolase‐II of during hydrolysis of microcrystalline cellulose publication-title: Biotechnol Bioeng – volume: 16 start-page: 566 issue: 6 year: 2000 end-page: 567 article-title: DaliLite workbench for protein structure comparison publication-title: Bioinformatics – ident: e_1_2_1_24_1 doi: 10.1007/BF02920125 – ident: e_1_2_1_9_1 doi: 10.1016/S1369-5266(99)00039-4 – ident: e_1_2_1_16_1 doi: 10.1002/bit.260420811 – ident: e_1_2_1_37_1 doi: 10.1073/pnas.0605979103 – ident: e_1_2_1_36_1 doi: 10.1002/bit.20942 – ident: e_1_2_1_20_1 doi: 10.1073/pnas.91.14.6574 – ident: e_1_2_1_27_1 doi: 10.1038/427030a – ident: e_1_2_1_19_1 doi: 10.1038/nbt0208-169 – ident: e_1_2_1_13_1 doi: 10.1016/S0960-8524(97)00103-X – ident: e_1_2_1_26_1 doi: 10.1002/jcc.20084 – ident: e_1_2_1_8_1 doi: 10.1038/35030000 – ident: e_1_2_1_34_1 doi: 10.1042/bj2550895 – ident: e_1_2_1_22_1 doi: 10.1007/10_2007_066 – ident: e_1_2_1_23_1 doi: 10.1002/bit.21856 – volume-title: Measurement of cellulase activities, Chemical Analysis and Testing Task: 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| Snippet | Expansin is a plant protein family that induces plant cell wall-loosening and cellulose disruption without exerting cellulose-hydrolytic activity.... Expansin is a plant protein family that induces plant cell wall‐loosening and cellulose disruption without exerting cellulose‐hydrolytic activity.... |
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| SubjectTerms | Amino Acid Sequence Bacillus subtilis Bacillus subtilis - enzymology Bacillus subtilis - genetics Bacteria bacterial expansin Bacterial Proteins - genetics Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Bacteriology Biodiesel fuels biofuel Biological and medical sciences Biotechnology cellulase Cellulase - metabolism Cellulose Cellulose - metabolism cellulose hydrolysis Cloning, Molecular E coli Enzymes Enzymes - genetics Enzymes - isolation & purification Enzymes - metabolism Escherichia coli - genetics Eukaryotes Fundamental and applied biological sciences. Psychology Gene Expression Genes Hydrolysis Models, Molecular Molecular Sequence Data Nematoda Protein Structure, Tertiary Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Sequence Homology, Amino Acid structural homolog Synergism Synergistic effect Zea mays |
| Title | Functional characterization of a bacterial expansin from Bacillus subtilis for enhanced enzymatic hydrolysis of cellulose |
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