메뉴 건너뛰기




Volumn 115, Issue 6, 2013, Pages 618-622

Alkalophilic adaptation of XynB endoxylanase from Aspergillus niger via rational design of pKa of catalytic residues

Author keywords

Alkalophilic adaptation; Aspergillus niger; Endoxylanase; PH stability; Rational design

Indexed keywords

ALKALOPHILIC; ASPERGILLUS NIGER; ENDOXYLANASE; PH-STABILITY; RATIONAL DESIGN;

EID: 84876974824     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2012.12.006     Document Type: Article
Times cited : (19)

References (25)
  • 1
    • 0037385801 scopus 로고    scopus 로고
    • Thermomyces lanuginosus: properties of strains and their hemicelluloses
    • Singh S., Madlala A.M., Prior B.A. Thermomyces lanuginosus: properties of strains and their hemicelluloses. FEMS Microbiol. Rev. 2003, 27:3-16.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 3-16
    • Singh, S.1    Madlala, A.M.2    Prior, B.A.3
  • 2
    • 0025804758 scopus 로고
    • Domains in microbial β-1,4-glycanases: sequence conservation, function, and enzyme families
    • Gilkes N.R., Henrissat B., Kilburn D.G., Miller R.C., Warren R.A.J. 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
  • 4
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B., Bairoch A. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 1993, 293:781-788.
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 5
    • 0028338985 scopus 로고
    • Three-dimensional structure of endo-1,4-β-xylanase II from Trichoderma reesei: two conformational states in the active site
    • Torronen A., Harkki A., Rouvinen J. Three-dimensional structure of endo-1,4-β-xylanase II from Trichoderma reesei: two conformational states in the active site. EMBO J. 1994, 13:2493-2501.
    • (1994) EMBO J. , vol.13 , pp. 2493-2501
    • Torronen, A.1    Harkki, A.2    Rouvinen, J.3
  • 6
    • 0033952763 scopus 로고    scopus 로고
    • Purification and properties of three endo-β-1,4-xylanases produced by Streptomyces sp. strain S38 which differ in their ability to enhance the bleaching of kraft pulps
    • Georis J., Giannotta F., Buyl E.D., Granier B., Frere J.M. Purification and properties of three endo-β-1,4-xylanases produced by Streptomyces sp. strain S38 which differ in their ability to enhance the bleaching of kraft pulps. Enzyme Microb. Technol. 2000, 26:178-186.
    • (2000) Enzyme Microb. Technol. , vol.26 , pp. 178-186
    • Georis, J.1    Giannotta, F.2    Buyl, E.D.3    Granier, B.4    Frere, J.M.5
  • 9
    • 12144282020 scopus 로고    scopus 로고
    • Xylanases, xylanase families and extremophilic xylanases
    • Collins T., Gerday C., Feller G. Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol. Rev. 2005, 29:3-23.
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 3-23
    • Collins, T.1    Gerday, C.2    Feller, G.3
  • 10
    • 0035723208 scopus 로고    scopus 로고
    • Directed evolution to produce an alkalophilc variant from a Neocallimastix pariciarum xylanase
    • Chen Y., Tang T., Cheng K. Directed evolution to produce an alkalophilc variant from a Neocallimastix pariciarum xylanase. Can. J. Microbiol. 2001, 47:1088-1094.
    • (2001) Can. J. Microbiol. , vol.47 , pp. 1088-1094
    • Chen, Y.1    Tang, T.2    Cheng, K.3
  • 12
    • 1942537597 scopus 로고    scopus 로고
    • Acidophilic adaptation of family 11 endo-beta-1,4-xylanases: modeling and mutational analysis
    • de Lemos Esteves F., Ruelle V., Lamotte-Brasseur J., Quinting B., Frère J.M. Acidophilic adaptation of family 11 endo-beta-1,4-xylanases: modeling and mutational analysis. Protein Sci. 2004, 13:1209-1218.
    • (2004) Protein Sci. , vol.13 , pp. 1209-1218
    • de Lemos Esteves, F.1    Ruelle, V.2    Lamotte-Brasseur, J.3    Quinting, B.4    Frère, J.M.5
  • 13
    • 76849098696 scopus 로고    scopus 로고
    • Computational design-based molecular engineering of the glycosyl hydrolase family 11 B. subtilis XynA endoxylanase improves its acid stability
    • Beliën T., Joye I.J., Delcour J.A., Courtin C.M. Computational design-based molecular engineering of the glycosyl hydrolase family 11 B. subtilis XynA endoxylanase improves its acid stability. Protein Eng. Des. Sel. 2009, 22:587-596.
    • (2009) Protein Eng. Des. Sel. , vol.22 , pp. 587-596
    • Beliën, T.1    Joye, I.J.2    Delcour, J.A.3    Courtin, C.M.4
  • 14
    • 0030592470 scopus 로고    scopus 로고
    • Three-dimensional structure of endo-1,4-xylanase I from Aspergillus niger: molecular basis for its low pH optimum
    • Krengel U., Dijkstra B.W. Three-dimensional structure of endo-1,4-xylanase I from Aspergillus niger: molecular basis for its low pH optimum. J. Mol. Biol. 1996, 263:70-78.
    • (1996) J. Mol. Biol. , vol.263 , pp. 70-78
    • Krengel, U.1    Dijkstra, B.W.2
  • 15
    • 0031008171 scopus 로고    scopus 로고
    • Cloning of two β-xylanase encoding genes from Aspergillu niger and their expression in Saccharomyces cerevisiae
    • Luttig M., Pretorius I.S., Van-Zyl W.H. Cloning of two β-xylanase encoding genes from Aspergillu niger and their expression in Saccharomyces cerevisiae. Biotechnol. Lett. 1997, 19:411-415.
    • (1997) Biotechnol. Lett. , vol.19 , pp. 411-415
    • Luttig, M.1    Pretorius, I.S.2    Van-Zyl, W.H.3
  • 16
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K., Bordoli L., Kopp J., Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006, 22:195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 17
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modeling server
    • Schwede T., Kopp J., Guex N., Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 2003, 31:3381-3385.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 18
    • 4143103785 scopus 로고    scopus 로고
    • The dual nature of the wheat xylanase protein inhibitor XIP-I: structural basis for the inhibition of family 10 and family 11 xylanases
    • Payan F., Leone P., Porciero S., Gilbert H.J., Juge N., Roussel A. The dual nature of the wheat xylanase protein inhibitor XIP-I: structural basis for the inhibition of family 10 and family 11 xylanases. J. Biol. Chem. 2004, 279:36029-36037.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36029-36037
    • Payan, F.1    Leone, P.2    Porciero, S.3    Gilbert, H.J.4    Juge, N.5    Roussel, A.6
  • 19
    • 79951476387 scopus 로고    scopus 로고
    • PROPKA3: consistent treatment of internal and surface residues in empirical pKa predictions
    • Mats H.M.O., Chresten R.S., Rostkowski M., Jan H.J. PROPKA3: consistent treatment of internal and surface residues in empirical pKa predictions. J. Chem. Theory Comput. 2011, 7:525-537.
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 525-537
    • Mats, H.M.O.1    Chresten, R.S.2    Rostkowski, M.3    Jan, H.J.4
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 1959, 31:426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 24
    • 0034716940 scopus 로고    scopus 로고
    • Hydrogen bonding and catalysis: a novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase
    • Joshi M.D., Sidhu G., Pot I., Brayer G.D., Withers S.G., Mclntosh L.P. Hydrogen bonding and catalysis: a novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase. J. Mol. Biol. 2000, 299:255-279.
    • (2000) J. Mol. Biol. , vol.299 , pp. 255-279
    • Joshi, M.D.1    Sidhu, G.2    Pot, I.3    Brayer, G.D.4    Withers, S.G.5    Mclntosh, L.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.