A novel thermoacidophilic and thermostable endo-β-1,4-glucanase from Phialophora sp. G5: Its thermostability influenced by a distinct β-sheet and the carbohydrate-binding module

Applied Microbiology and Biotechnology

Volumn 95, Issue 4, 2012, Pages 947-955

  Zhao, Junqi ^a   Shi, Pengjun ^a   Huang, Huoqing ^a   Li, Zhongyuan ^a   Yuan, Tiezheng ^a   Yang, Peilong ^a   Luo, Huiying ^a   Bai, Yingguo ^a   Yao, Bin ^a  

^a INSTITUTE OF PLANT PROTECTION   (China)

Author keywords

Carbohydrate binding module (CBM); Endo 1,4 glucanase; Phialophora sp. G5; Thermostability

Indexed keywords

CARBOHYDRATE-BINDING MODULES; CATALYTIC MODULES; ENDOGLUCANASES; FOUR AMINO ACIDS; GLYCOSIDE HYDROLASES; LIGNOCELLULOSIC MATERIAL; N-TERMINALS; OPEN READING FRAME; P. PASTORIS; PH OPTIMA; PH STABILITY; PHIALOPHORA SP. G5; PICHIA PASTORIS; SPECIFIC ACTIVITY; THERMOSTABILITY; TRICHODERMA SP;

AMINO ACIDS; CARBOHYDRATES; CLONING; GENES;

ENZYME ACTIVITY;

CARBOHYDRATE BINDING PROTEIN; CELLULASE; GLYCOSIDASE; LIGNOCELLULOSE;

CARBOHYDRATE; CELLULOSE; ENZYME ACTIVITY; FUNGUS; LIGNIN; MUTATION; PH; RECOMBINATION; TEMPERATURE EFFECT;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; BIOTRANSFORMATION; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; FUNGUS MUTANT; GENE CONSTRUCT; HYPHOMYCETES; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PH; PICHIA PASTORIS; PROTEIN EXPRESSION; PROTEIN FUNCTION; SEQUENCE ANALYSIS; THERMOACIDOPHILIC BACTERIUM; THERMOSTABILITY; TRICHODERMA;

AMINO ACID SEQUENCE; BASE SEQUENCE; CARBOHYDRATE METABOLISM; CELLULASE; CIRCULAR DICHROISM; CLONING, MOLECULAR; DNA, FUNGAL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME STABILITY; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHIALOPHORA; SUBSTRATE SPECIFICITY;

FUNGI; PHIALOPHORA; PICHIA PASTORIS; TRICHODERMA SP. C-4;

EID: 84864609239     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-011-3807-0     Document Type: Article

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