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Volumn 123, Issue , 2012, Pages 125-134

Structural modeling and further improvement in pH stability and activity of a highly-active xylanase from an uncultured rumen fungus

Author keywords

Molecular modeling; Neocallimastix; Rumen fungus; Site directed mutagenesis; Xylanase

Indexed keywords

BIOFUEL PRODUCTION; FUNGAL CULTURE; GLYCOSYL HYDROLASES; MUTANT ENZYMES; NEOCALLIMASTIX; PH STABILITY; PHYLOGENETIC ANALYSIS; SITE DIRECTED MUTAGENESIS; STRUCTURAL MODELING; XYLANASES;

EID: 84865552264     PISSN: 09608524     EISSN: 18732976     Source Type: Journal    
DOI: 10.1016/j.biortech.2012.05.142     Document Type: Article
Times cited : (19)

References (23)
  • 2
    • 61449242659 scopus 로고    scopus 로고
    • The identification, purification, and characterization of STXF10 expressed in Streptomyces thermonitrificans NTU-88
    • Cheng H.L., Tsai C.Y., Chen H.J., Yang S.S., Chen Y.C. The identification, purification, and characterization of STXF10 expressed in Streptomyces thermonitrificans NTU-88. Appl. Microbiol. Biotechnol. 2009, 82:681-689.
    • (2009) Appl. Microbiol. Biotechnol. , vol.82 , pp. 681-689
    • Cheng, H.L.1    Tsai, C.Y.2    Chen, H.J.3    Yang, S.S.4    Chen, Y.C.5
  • 3
    • 0037047015 scopus 로고    scopus 로고
    • Mutagenesis of Trp54 and Trp203 residues on Fibrobacter succinogenes 1,3-1,4-beta-d-glucanase significantly affects catalytic activities of the enzyme
    • Cheng H.L., Tsai L.C., Lin S.S., Yuan H.S., Yang N.S., Lee S.H., Shyur L.F. Mutagenesis of Trp54 and Trp203 residues on Fibrobacter succinogenes 1,3-1,4-beta-d-glucanase significantly affects catalytic activities of the enzyme. Biochemistry 2002, 41:8759-8766.
    • (2002) Biochemistry , vol.41 , pp. 8759-8766
    • Cheng, H.L.1    Tsai, L.C.2    Lin, S.S.3    Yuan, H.S.4    Yang, N.S.5    Lee, S.H.6    Shyur, L.F.7
  • 4
    • 34848868504 scopus 로고    scopus 로고
    • Cloning, characterization and phylogenetic relationships of stxI, a endoxylanase-encoding gene from Streptomyces thermonitrificans NTU-88
    • Cheng H.L., Wang P.M., Yang S.S., Chen Y.C. Cloning, characterization and phylogenetic relationships of stxI, a endoxylanase-encoding gene from Streptomyces thermonitrificans NTU-88. Bioresour. Technol. 2008, 99:227-231.
    • (2008) Bioresour. Technol. , vol.99 , pp. 227-231
    • Cheng, H.L.1    Wang, P.M.2    Yang, S.S.3    Chen, Y.C.4
  • 5
    • 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
  • 6
    • 64849094324 scopus 로고    scopus 로고
    • Cellulosic ethanol production from sugarcane bagasse without enzymatic saccharification
    • Dawson L., Boopathy R. Cellulosic ethanol production from sugarcane bagasse without enzymatic saccharification. Bioresources 2008, 3:452-460.
    • (2008) Bioresources , vol.3 , pp. 452-460
    • Dawson, L.1    Boopathy, R.2
  • 8
    • 0032407988 scopus 로고    scopus 로고
    • Crystallographic and mutational analyses of an extremely acidophilic and acid-stable xylanase: biased distribution of acidic residues and importance of Asp37 for catalysis at low pH
    • Fushinobu S., Ito K., Konno M., Wakagi T., Matsuzawa H. Crystallographic and mutational analyses of an extremely acidophilic and acid-stable xylanase: biased distribution of acidic residues and importance of Asp37 for catalysis at low pH. Protein Eng. 1998, 11:1121-1128.
    • (1998) Protein Eng. , vol.11 , pp. 1121-1128
    • Fushinobu, S.1    Ito, K.2    Konno, M.3    Wakagi, T.4    Matsuzawa, H.5
  • 10
    • 49449102763 scopus 로고    scopus 로고
    • Substrate dependency and effect of xylanase supplementation on enzymatic hydrolysis of ammonia-treated biomass
    • Gupta R., Kim T.H., Lee Y.Y. Substrate dependency and effect of xylanase supplementation on enzymatic hydrolysis of ammonia-treated biomass. Appl. Biochem. Biotechnol. 2008, 148:59-70.
    • (2008) Appl. Biochem. Biotechnol. , vol.148 , pp. 59-70
    • Gupta, R.1    Kim, T.H.2    Lee, Y.Y.3
  • 11
    • 15944395067 scopus 로고    scopus 로고
    • Effects of dockerin domains on Neocallimastix frontalis xylanases
    • Huang Y.H., Huang C.T., Hseu R.S. Effects of dockerin domains on Neocallimastix frontalis xylanases. FEMS Microbiol. Lett. 2005, 243:455-460.
    • (2005) FEMS Microbiol. Lett. , vol.243 , pp. 455-460
    • Huang, Y.H.1    Huang, C.T.2    Hseu, R.S.3
  • 12
    • 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., McIntosh 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    McIntosh, L.P.6
  • 13
    • 25644456926 scopus 로고    scopus 로고
    • Direct cloning of a xylanase gene from the mixed genomic DNA of rumen fungi and its expression in intestinal Lactobacillus reuteri
    • Liu J.R., Yu B., Lin S.H., Cheng K.J., Chen Y.C. Direct cloning of a xylanase gene from the mixed genomic DNA of rumen fungi and its expression in intestinal Lactobacillus reuteri. FEMS Microbiol. Lett. 2005, 251:233-241.
    • (2005) FEMS Microbiol. Lett. , vol.251 , pp. 233-241
    • Liu, J.R.1    Yu, B.2    Lin, S.H.3    Cheng, K.J.4    Chen, Y.C.5
  • 15
    • 0030269964 scopus 로고    scopus 로고
    • The rumen: a unique source of enzymes for enhancing livestock production
    • Selinger L.B., Forsberg C.W., Cheng K.J. The rumen: a unique source of enzymes for enhancing livestock production. Anaerobe 1996, 2:263-284.
    • (1996) Anaerobe , vol.2 , pp. 263-284
    • Selinger, L.B.1    Forsberg, C.W.2    Cheng, K.J.3
  • 16
    • 80052379049 scopus 로고    scopus 로고
    • Evaluation of hemicellulose removal by xylanase and delignification on SHF and SSF for bioethanol production with steam-pretreated substrates
    • Shen F., Kumar L., Hu J., Saddler J.N. Evaluation of hemicellulose removal by xylanase and delignification on SHF and SSF for bioethanol production with steam-pretreated substrates. Bioresour. Technol. 2011, 102:8945-8951.
    • (2011) Bioresour. Technol. , vol.102 , pp. 8945-8951
    • Shen, F.1    Kumar, L.2    Hu, J.3    Saddler, J.N.4
  • 17
    • 0003149785 scopus 로고    scopus 로고
    • Adsorption of Clostridium stercorarium xylanase A to insoluble xylan and the importance of the CBDs to xylan hydrolysis
    • Sun J.L., Sakka K., Karita S., Kimura T., Ohmiya K. Adsorption of Clostridium stercorarium xylanase A to insoluble xylan and the importance of the CBDs to xylan hydrolysis. J. Ferment. Bioeng. 1998, 85:63-68.
    • (1998) J. Ferment. Bioeng. , vol.85 , pp. 63-68
    • Sun, J.L.1    Sakka, K.2    Karita, S.3    Kimura, T.4    Ohmiya, K.5
  • 18
    • 84858707775 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a highly thermostable xylanase from Actinomadura sp. strain Cpt20 isolated from poultry compost
    • Taibi Z., Saoudi B., Boudelaa M., Trigui H., Belghith H., Gargouri A., Ladjama A. Purification and biochemical characterization of a highly thermostable xylanase from Actinomadura sp. strain Cpt20 isolated from poultry compost. Appl. Biochem. Biotechnol. 2012, 166:663-679.
    • (2012) Appl. Biochem. Biotechnol. , vol.166 , pp. 663-679
    • Taibi, Z.1    Saoudi, B.2    Boudelaa, M.3    Trigui, H.4    Belghith, H.5    Gargouri, A.6    Ladjama, A.7
  • 19
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0
    • Tamura K., Dudley J., Nei M., Kumar S. MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol. Biol. Evol. 2007, 24:1596-1599.
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 20
    • 0040003315 scopus 로고    scopus 로고
    • Structural and functional properties of low molecular weight endo-1,4-beta-xylanases
    • Torronen A., Rouvinen J. Structural and functional properties of low molecular weight endo-1,4-beta-xylanases. J. Biotechnol. 1997, 57:137-149.
    • (1997) J. Biotechnol. , vol.57 , pp. 137-149
    • Torronen, A.1    Rouvinen, J.2
  • 22
    • 84856572462 scopus 로고    scopus 로고
    • Cloning, expression and applicability of thermo-alkali-stable xylanase of Geobacillus thermoleovorans in generating xylooligosaccharides from agro-residues
    • Verma D., Satyanarayana T. Cloning, expression and applicability of thermo-alkali-stable xylanase of Geobacillus thermoleovorans in generating xylooligosaccharides from agro-residues. Bioresour. Technol. 2012, 107:333-338.
    • (2012) Bioresour. Technol. , vol.107 , pp. 333-338
    • Verma, D.1    Satyanarayana, T.2
  • 23
    • 78650821698 scopus 로고    scopus 로고
    • A novel cold-active xylanase gene from the environmental DNA of goat rumen contents: direct cloning, expression and enzyme characterization
    • Wang G., Luo H., Wang Y., Huang H., Shi P., Yang P., Meng K., Bai Y., Yao B. A novel cold-active xylanase gene from the environmental DNA of goat rumen contents: direct cloning, expression and enzyme characterization. Bioresour. Technol. 2011, 102:3330-3336.
    • (2011) Bioresour. Technol. , vol.102 , pp. 3330-3336
    • Wang, G.1    Luo, H.2    Wang, Y.3    Huang, H.4    Shi, P.5    Yang, P.6    Meng, K.7    Bai, Y.8    Yao, B.9


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