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Volumn 10, Issue , 2011, Pages

A thermostable GH45 endoglucanase from yeast: Impact of its atypical multimodularity on activity

Author keywords

Biomass; Cellulase; Crystalline cellulose; Pichia pastoris; Thermostable gh45 endoglucanase

Indexed keywords

CELLOHEXAOSE; CELLULOSE; CRYSTALLINE CELLULOSE; GLUCAN; GLUCAN SYNTHASE; GLYCOSIDE HYDROLASE FAMILY 45 ENDOGLUCANASE; UNCLASSIFIED DRUG; FUNGAL PROTEIN; GLYCOSIDASE;

EID: 82655177621     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-10-103     Document Type: Article
Times cited : (41)

References (52)
  • 3
    • 58249085751 scopus 로고    scopus 로고
    • Lignocellulosic residues: biodegradation and bioconversion by fungi
    • Sánchez C. Lignocellulosic residues: biodegradation and bioconversion by fungi. Biotechnol Adv 2009, 27:185-194.
    • (2009) Biotechnol Adv , vol.27 , pp. 185-194
    • Sánchez, C.1
  • 4
    • 84966185447 scopus 로고
    • Synergism of Cellulases from Trichoderma reesei in the degradation of cellulose
    • Henrissat B, Driguez H, Viet C, Schülein M. Synergism of Cellulases from Trichoderma reesei in the degradation of cellulose. Nature Biotechnol 1985, 3:722-726.
    • (1985) Nature Biotechnol , vol.3 , pp. 722-726
    • Henrissat, B.1    Driguez, H.2    Viet, C.3    Schülein, M.4
  • 7
    • 84881089389 scopus 로고    scopus 로고
    • CAZy database
    • CAZy database. , http://www.CAZy.org
  • 10
    • 0037048802 scopus 로고    scopus 로고
    • Enzymatic properties of the low molecular mass endoglucanases Cel12A (EG III) and Cel45A (EG V) of Trichoderma reesei
    • Karlsson J, Siika-Aho M, Tenkanen M, Tjerneld F. Enzymatic properties of the low molecular mass endoglucanases Cel12A (EG III) and Cel45A (EG V) of Trichoderma reesei. J Biotechno 2002, 99:63-78.
    • (2002) J Biotechno , vol.99 , pp. 63-78
    • Karlsson, J.1    Siika-Aho, M.2    Tenkanen, M.3    Tjerneld, F.4
  • 11
    • 0025804758 scopus 로고
    • Domains in microbial β-1,4-glycanases: sequence conservation, function, and enzyme families
    • Gilkes NR, Henrissat B, Kilburn DG, Miller RC, Warren RAJ. Domains in microbial β-1,4-glycanases: sequence conservation, function, and enzyme families. Microbiol Rev 1991, 55:303-315.
    • (1991) Microbiol Rev , vol.55 , pp. 303-315
    • Gilkes, N.R.1    Henrissat, B.2    Kilburn, D.G.3    Miller, R.C.4    Warren, R.A.J.5
  • 13
    • 47349122440 scopus 로고    scopus 로고
    • A novel function for the cellulose-binding module of cellobiohydrolase I
    • Wang L, Zhang Y, Gao P. A novel function for the cellulose-binding module of cellobiohydrolase I. Sci China C Life Sci 2008, 51:620-629.
    • (2008) Sci China C Life Sci , vol.51 , pp. 620-629
    • Wang, L.1    Zhang, Y.2    Gao, P.3
  • 14
    • 77649287391 scopus 로고    scopus 로고
    • Access to cellulose limits the efficiency of enzymatic hydrolysis: the role of amorphogenesis
    • Arantes V, Saddler JN. Access to cellulose limits the efficiency of enzymatic hydrolysis: the role of amorphogenesis. Biotechnol Biofuels 2010, 23:3-4.
    • (2010) Biotechnol Biofuels , vol.23 , pp. 3-4
    • Arantes, V.1    Saddler, J.N.2
  • 15
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: fine-tuning polysaccharide recognition
    • Boraston AB, Bolam DN, Gilbert HJ, Davies GJ. Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem J 2004, 382:769-781.
    • (2004) Biochem J , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 17
    • 0030724903 scopus 로고    scopus 로고
    • Molecular characterization of the alpha-amylase genes of Lactobacillus plantarum A6 and Lactobacillus amylovorus reveals an unusual 3' end structure with direct tandem repeats and suggests a common evolutionary origin
    • Giraud E, Cuny T. Molecular characterization of the alpha-amylase genes of Lactobacillus plantarum A6 and Lactobacillus amylovorus reveals an unusual 3' end structure with direct tandem repeats and suggests a common evolutionary origin. Gene 1997, 198:149-157.
    • (1997) Gene , vol.198 , pp. 149-157
    • Giraud, E.1    Cuny, T.2
  • 18
    • 17644417083 scopus 로고    scopus 로고
    • Alternative splicing produces two endoglucanases with one or two CBM in Mucor circinelloides
    • Baba Y, Shimonaka A, Koga J, Kubota H, Kono T. Alternative splicing produces two endoglucanases with one or two CBM in Mucor circinelloides. J Bacteriol 2005, 187:3045-3051.
    • (2005) J Bacteriol , vol.187 , pp. 3045-3051
    • Baba, Y.1    Shimonaka, A.2    Koga, J.3    Kubota, H.4    Kono, T.5
  • 20
    • 0033670249 scopus 로고    scopus 로고
    • Horizontal gene transfer in bacterial and archaeal complete genomes
    • Garcia-Vallvé S, Romeu A, Palau J. Horizontal gene transfer in bacterial and archaeal complete genomes. Genome Res 2000, 10:1719-1725.
    • (2000) Genome Res , vol.10 , pp. 1719-1725
    • Garcia-Vallvé, S.1    Romeu, A.2    Palau, J.3
  • 21
    • 38349128431 scopus 로고    scopus 로고
    • Purification and characterization of recombinant endoglucanase of Trichoderma reesei expressed in Saccharomyces cerevisiae with higher glycosylation and stability
    • Qin Y, Wei X, Liu X, Wang T, Qu Y. Purification and characterization of recombinant endoglucanase of Trichoderma reesei expressed in Saccharomyces cerevisiae with higher glycosylation and stability. Protein Expr Purif 2008, 58(1):162-167.
    • (2008) Protein Expr Purif , vol.58 , Issue.1 , pp. 162-167
    • Qin, Y.1    Wei, X.2    Liu, X.3    Wang, T.4    Qu, Y.5
  • 22
    • 77954708183 scopus 로고    scopus 로고
    • Characterization of the endoglucanase and glucomannanase activities of a glycoside hydrolase family 45 protein from Penicillium decumbens
    • Liu G, Wei X, Qin Y, Qu Y. Characterization of the endoglucanase and glucomannanase activities of a glycoside hydrolase family 45 protein from Penicillium decumbens. J Gen Appl Microbiol 2010, 56:223-229.
    • (2010) J Gen Appl Microbiol , vol.56 , pp. 223-229
    • Liu, G.1    Wei, X.2    Qin, Y.3    Qu, Y.4
  • 23
    • 34347250861 scopus 로고    scopus 로고
    • Characterization of a family 45 glycosyl hydrolase from Fibrobacter succinogenes S85
    • Seon Park J, Russell JB, Wilson DB. Characterization of a family 45 glycosyl hydrolase from Fibrobacter succinogenes S85. Anaerobe 2007, 13(2):83-88.
    • (2007) Anaerobe , vol.13 , Issue.2 , pp. 83-88
    • Seon Park, J.1    Russell, J.B.2    Wilson, D.B.3
  • 25
    • 33746614259 scopus 로고    scopus 로고
    • Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls
    • Bauer S, Vasu P, Persson S, Mort AJ, Somerville CR. Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls. Proc Natl Acad Sci USA 2006, 103(30):11417-11422.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.30 , pp. 11417-11422
    • Bauer, S.1    Vasu, P.2    Persson, S.3    Mort, A.J.4    Somerville, C.R.5
  • 26
    • 71049124032 scopus 로고    scopus 로고
    • Cloning, expression in Pichia pastoris, and characterization of a thermostable GH5 mannan endo-1,4-beta-mannosidase from Aspergillus niger BK01
    • Do BC, Dang TT, Berrin JG, Haltrich D, To KA, Sigoillot JC, Yamabhai M. Cloning, expression in Pichia pastoris, and characterization of a thermostable GH5 mannan endo-1,4-beta-mannosidase from Aspergillus niger BK01. Microb Cell Fact 2009, 8:59.
    • (2009) Microb Cell Fact , vol.8 , pp. 59
    • Do, B.C.1    Dang, T.T.2    Berrin, J.G.3    Haltrich, D.4    To, K.A.5    Sigoillot, J.C.6    Yamabhai, M.7
  • 27
    • 79251613225 scopus 로고    scopus 로고
    • Podospora anserina hemicellulases potentiate the Trichoderma reesei secretome for saccharification of lignocellulosic biomass
    • Couturier M, Haon M, Coutinho PM, Henrissat B, Lesage-Meessen L, Berrin JG. Podospora anserina hemicellulases potentiate the Trichoderma reesei secretome for saccharification of lignocellulosic biomass. Appl Environ Microbiol 2011, 77(1):237-246.
    • (2011) Appl Environ Microbiol , vol.77 , Issue.1 , pp. 237-246
    • Couturier, M.1    Haon, M.2    Coutinho, P.M.3    Henrissat, B.4    Lesage-Meessen, L.5    Berrin, J.G.6
  • 28
    • 52649091899 scopus 로고    scopus 로고
    • Characterization of an endoglucanase belonging to a new subfamily of glycoside hydrolase family 45 of the basidiomycete Phanerochaete chrysosporium
    • Igarashi K, Ishida T, Hori C, Samejima M. Characterization of an endoglucanase belonging to a new subfamily of glycoside hydrolase family 45 of the basidiomycete Phanerochaete chrysosporium. Appl Environ Microbiol 2008, 74:5628-5634.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 5628-5634
    • Igarashi, K.1    Ishida, T.2    Hori, C.3    Samejima, M.4
  • 29
    • 45749083300 scopus 로고    scopus 로고
    • Purification and characterization of recombinant endoglucanases from the pine wood nematode Bursaphelenchus xylophilus
    • Shibuya H, Kikuchi T. Purification and characterization of recombinant endoglucanases from the pine wood nematode Bursaphelenchus xylophilus. Biosc Biotechnol Biochem 2008, 72:1325-1332.
    • (2008) Biosc Biotechnol Biochem , vol.72 , pp. 1325-1332
    • Shibuya, H.1    Kikuchi, T.2
  • 31
    • 0027381121 scopus 로고
    • Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodextrins by nine cellulases
    • Schou C, Rasmussen G, Kaltoft MB, Henrissat B, Schülein M. Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodextrins by nine cellulases. Eur J Biochem 1993, 217:947-953.
    • (1993) Eur J Biochem , vol.217 , pp. 947-953
    • Schou, C.1    Rasmussen, G.2    Kaltoft, M.B.3    Henrissat, B.4    Schülein, M.5
  • 32
    • 0028822343 scopus 로고
    • Structures of oligosaccharide-bound forms of the endoglucanase V from Humicola insolens at 1.9 Å resolution
    • Davies GJ, Tolley SP, Henrissat B, Hjort C, Schülein M. Structures of oligosaccharide-bound forms of the endoglucanase V from Humicola insolens at 1.9 Å resolution. Biochemistry 1995, 34:16210-16220.
    • (1995) Biochemistry , vol.34 , pp. 16210-16220
    • Davies, G.J.1    Tolley, S.P.2    Henrissat, B.3    Hjort, C.4    Schülein, M.5
  • 34
    • 38549088955 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a thermotolerant endoglucanase from Syncephalastrum racemosum (BCC18080) in Pichia pastoris
    • Wonganu B, Pootanakit K, Boonyapakron K, Champreda V, Tanapongpipat S, Eurwilaichitr L. Cloning, expression and characterization of a thermotolerant endoglucanase from Syncephalastrum racemosum (BCC18080) in Pichia pastoris. Protein Expr Purif 2008, 58:78-86.
    • (2008) Protein Expr Purif , vol.58 , pp. 78-86
    • Wonganu, B.1    Pootanakit, K.2    Boonyapakron, K.3    Champreda, V.4    Tanapongpipat, S.5    Eurwilaichitr, L.6
  • 35
    • 78651083397 scopus 로고    scopus 로고
    • Cloning and characterization of a thermostable and halo-tolerant endoglucanase from Thermoanaerobacter tengcongensis MB4
    • Liang C, Xue Y, Fioroni M, Rodríguez-Ropero F, Zhou C, Schwaneberg U, Ma Y. Cloning and characterization of a thermostable and halo-tolerant endoglucanase from Thermoanaerobacter tengcongensis MB4. Appl Microbiol Biotechnol 2011, 89(2):315-326.
    • (2011) Appl Microbiol Biotechnol , vol.89 , Issue.2 , pp. 315-326
    • Liang, C.1    Xue, Y.2    Fioroni, M.3    Rodríguez-Ropero, F.4    Zhou, C.5    Schwaneberg, U.6    Ma, Y.7
  • 36
    • 77955050826 scopus 로고    scopus 로고
    • Hydrolysis of softwood by Aspergillus mannanase: role of a carbohydrate-binding module
    • Pham TA, Berrin JG, Record E, To KA, Sigoillot JC. Hydrolysis of softwood by Aspergillus mannanase: role of a carbohydrate-binding module. J Biotechnol 2010, 148:163-170.
    • (2010) J Biotechnol , vol.148 , pp. 163-170
    • Pham, T.A.1    Berrin, J.G.2    Record, E.3    To, K.A.4    Sigoillot, J.C.5
  • 37
    • 78651289576 scopus 로고    scopus 로고
    • The role of carbohydrate-binding module (CBM) repeat of a multimodular xylanase (XynX) from Clostridium thermocellum in cellulose and xylan binding
    • Selvaraj T, Kim SK, Kim YH, Jeong YS, Kim YJ, Phuong ND, Jung KH, Kim J, Yun HD, Kim H. The role of carbohydrate-binding module (CBM) repeat of a multimodular xylanase (XynX) from Clostridium thermocellum in cellulose and xylan binding. J Microbiol 2010, (48):(6):856-861.
    • (2010) J Microbiol , vol.48 , Issue.6 , pp. 856-861
    • Selvaraj, T.1    Kim, S.K.2    Kim, Y.H.3    Jeong, Y.S.4    Kim, Y.J.5    Phuong, N.D.6    Jung, K.H.7    Kim, J.8    Yun, H.D.9    Kim, H.10
  • 38
    • 0027651651 scopus 로고
    • Activity studies of eight purified cellulases: Specificity, synergism, and binding domain effects
    • Irwin DC, Spezio M, Walker LP, Wilson DB. Activity studies of eight purified cellulases: Specificity, synergism, and binding domain effects. Biotechnol Bioeng 1993, 42:1002-1013.
    • (1993) Biotechnol Bioeng , vol.42 , pp. 1002-1013
    • Irwin, D.C.1    Spezio, M.2    Walker, L.P.3    Wilson, D.B.4
  • 39
    • 0034283404 scopus 로고    scopus 로고
    • New type of starch-binding domain: the direct repeat motif in the C-terminal region of Bacillus sp. no. 195 alpha-amylase contributes to starch binding and raw starch degrading
    • Sumitani J, Tottori T, Kawaguchi T, Arai M. New type of starch-binding domain: the direct repeat motif in the C-terminal region of Bacillus sp. no. 195 alpha-amylase contributes to starch binding and raw starch degrading. Biochem J 2000, 350:477-484.
    • (2000) Biochem J , vol.350 , pp. 477-484
    • Sumitani, J.1    Tottori, T.2    Kawaguchi, T.3    Arai, M.4
  • 41
    • 77957330454 scopus 로고    scopus 로고
    • Engineered microbial systems for enhanced conversion of lignocellulosic biomass
    • Elkins JG, Raman B, Keller M. Engineered microbial systems for enhanced conversion of lignocellulosic biomass. Curr Opin Biotechnol 2010, 21:657-662.
    • (2010) Curr Opin Biotechnol , vol.21 , pp. 657-662
    • Elkins, J.G.1    Raman, B.2    Keller, M.3
  • 42
    • 34548710320 scopus 로고    scopus 로고
    • Consolidated bioprocessing for bioethanol production using Saccharomyces cerevisiae
    • van Zyl WH, Lynd LR, den Haan R, McBride JE. Consolidated bioprocessing for bioethanol production using Saccharomyces cerevisiae. Adv Biochem Eng Biotechnol 2007, 108:205-235.
    • (2007) Adv Biochem Eng Biotechnol , vol.108 , pp. 205-235
    • van Zyl, W.H.1    Lynd, L.R.2    den Haan, R.3    McBride, J.E.4
  • 43
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar RC. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 2004, 32:1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 45
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones DT, Taylor WR, Thornton JM. The rapid generation of mutation data matrices from protein sequences. Comput Appl Biosc 1992, 8:275-282.
    • (1992) Comput Appl Biosc , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 46
    • 84944178665 scopus 로고
    • Hierarchical grouping to optimize an objective function
    • Ward JH. Hierarchical grouping to optimize an objective function. J Am Stat Assoc 1963, 58:236-244.
    • (1963) J Am Stat Assoc , vol.58 , pp. 236-244
    • Ward, J.H.1
  • 47
    • 84855472323 scopus 로고    scopus 로고
    • Dendroscope 2.6.1
    • Dendroscope 2.6.1. , http://ab.inf.uni-tuebingen.de/software/dendroscope/
  • 50
    • 0036226314 scopus 로고    scopus 로고
    • Novel carbohydrate-binding module of beta-1,3-xylanase from a marine bacterium, Alcaligenes sp. strain XY-234
    • Okazaki F, Tamaru Y, Hashikawa S, Li YT, Araki T. Novel carbohydrate-binding module of beta-1,3-xylanase from a marine bacterium, Alcaligenes sp. strain XY-234. J Bacteriol 2002, 184(9):2399-2403.
    • (2002) J Bacteriol , vol.184 , Issue.9 , pp. 2399-2403
    • Okazaki, F.1    Tamaru, Y.2    Hashikawa, S.3    Li, Y.T.4    Araki, T.5
  • 51
    • 0025729215 scopus 로고
    • Subsite structure of Saccharomycopsis alpha-amylase secreted from Saccharomyces cerevisiae
    • Matsui I, Ishikawa K, Matsui E, Miyairi S, Fukui S, Honda K. Subsite structure of Saccharomycopsis alpha-amylase secreted from Saccharomyces cerevisiae. J Biochem 1991, 109:566-569.
    • (1991) J Biochem , vol.109 , pp. 566-569
    • Matsui, I.1    Ishikawa, K.2    Matsui, E.3    Miyairi, S.4    Fukui, S.5    Honda, K.6
  • 52
    • 33947215205 scopus 로고    scopus 로고
    • Substrate and product hydrolysis specificity in family 11 glycoside hydrolase: an analysis of Penicillium funiculosum and Penicillum griseofulvum xylanases
    • Berrin JG, Ajandouz el H, Georis J, Arnaut F, Juge N. Substrate and product hydrolysis specificity in family 11 glycoside hydrolase: an analysis of Penicillium funiculosum and Penicillum griseofulvum xylanases. Appl Microbiol Biotechnol 2007, 74(5):1001-1010.
    • (2007) Appl Microbiol Biotechnol , vol.74 , Issue.5 , pp. 1001-1010
    • Berrin, J.G.1    Ajandouz el, H.2    Georis, J.3    Arnaut, F.4    Juge, N.5


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