Three amino acid changes contribute markedly to the thermostability of β-glucosidase BglC from Thermobifida fusca

Bioresource Technology

Volumn 102, Issue 3, 2011, Pages 3337-3342

  Pei, Xiao Qiong ^a   Yi, Zhuo Lin ^a,b   Tang, Chuan Gen ^a,b   Wu, Zhong Liu ^a  

^a CHENGDU INSTITUTE OF BIOLOGY   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

Directed evolution; Family shuffling; Glucosidase; Saturation mutagenesis; Thermostability

Indexed keywords

DIRECTED EVOLUTION; FAMILY SHUFFLING; GLUCOSIDASE; SATURATION MUTAGENESIS; THERMOSTABILITY;

AMINO ACIDS; ENZYMES;

MUTAGENESIS;

BACTERIAL PROTEIN; BETA GLUCOSIDASE; CELLOBIOSE; GLUCOPYRANOSIDE; PROTEIN BGLB; PROTEIN BGLC; UNCLASSIFIED DRUG;

AMINO ACID; BIOMASS; BIOTRANSFORMATION; ENZYME ACTIVITY; EVOLUTIONARY BIOLOGY; HALF LIFE; MOLECULAR ANALYSIS; MUTATION; RECYCLING; SATURATION; TEMPERATURE TOLERANCE; THERMOPHILIC BACTERIUM;

ACTINOBACTERIA; AMINO ACID ANALYSIS; ARTICLE; BIOMASS CONVERSION; CONTROLLED STUDY; DNA SHUFFLING; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME SUBSTRATE; HALF LIFE TIME; HIGH THROUGHPUT SCREENING; MICROBIAL BIOMASS; NONHUMAN; PAEBIBACILLUS POLYMXYXA; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTEIN SYNTHESIS; SITE DIRECTED MUTAGENESIS; STREPTOMYCES; THERMOBIFIDA FUSCA; THERMOSTABILITY;

ACTINOMYCETALES; AMINO ACID SUBSTITUTION; BETA-GLUCOSIDASE; ENZYME STABILITY; HOT TEMPERATURE; MUTAGENESIS, SITE-DIRECTED; PROTEIN ENGINEERING; STRUCTURE-ACTIVITY RELATIONSHIP;

THERMOBIFIDA FUSCA;

EID: 78650837146     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2010.11.025     Document Type: Article

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