Structure-based engineering of histidine residues in the catalytic domain of α-amylase from Bacillus subtilis for improved protein stability and catalytic efficiency under acidic conditions

Journal of Biotechnology

Volumn 164, Issue 1, 2013, Pages 59-66

  Yang, Haiquan ^a   Liu, Long ^a   Shin, Hyun Dong ^b   Chen, Rachel R ^b   Li, Jianghua ^a   Du, Guocheng ^a   Chen, Jian ^a  

^a JIANGNAN UNIVERSITY   (China)

^b Georgia Institute of Technology   (United States)

Author keywords

Acidic stability; Bacillus subtilis amylase; Site directed mutagenesis; Structure model

Indexed keywords

ACIDIC CONDITIONS; ACIDIC STABILITIES; BACILLUS SUBTILIS; CATALYTIC EFFICIENCIES; HISTIDINE RESIDUES; SITE DIRECTED MUTAGENESIS; STRUCTURE MODELS; THREE-DIMENSIONAL STRUCTURE;

AMINO ACIDS; EFFICIENCY; HYDROGEN BONDS; PROTEINS; STABILITY; THREE DIMENSIONAL;

AMYLASES;

AMYLASE; ASPARTIC ACID; HISTIDINE;

ACIDITY; ARTICLE; BACILLUS SUBTILIS; CATALYSIS; CLONING; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME PURIFICATION; ENZYME SYNTHESIS; GENE EXPRESSION; GENE MUTATION; HYDROGEN BOND; MUTANT; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN ENGINEERING; PROTEIN STABILITY; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; THREE DIMENSIONAL IMAGING; WILD TYPE;

ALPHA-AMYLASES; BACILLUS SUBTILIS; CATALYTIC DOMAIN; CLONING, MOLECULAR; ESCHERICHIA COLI; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MUTAGENESIS, SITE-DIRECTED; PROTEIN STABILITY; STRUCTURE-ACTIVITY RELATIONSHIP;

BACILLUS SUBTILIS;

EID: 84875092633     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2012.12.007     Document Type: Article

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