Assembly of mutations for improving thermostability of Escherichia coli AppA2 phytase

Applied Microbiology and Biotechnology

Volumn 79, Issue 5, 2008, Pages 751-758

  Kim, Moon Soo ^a,b   Weaver, Jeremy D ^a   Lei, Xin Gen ^a  

^a Department of Molecular Biology and Genetics   (United States)

^b PURDUE UNIVERSITY   (United States)

Author keywords

Enzyme; Phytase; Protein engineering; Structure; Thermostability

Indexed keywords

COULOMB INTERACTIONS; ENZYME ACTIVITY; PROTEINS; THERMODYNAMIC STABILITY;

PROTEIN ENGINEERING; SYNERGISTIC EFFECTS;

ESCHERICHIA COLI;

BACTERIAL ENZYME; ESCHERICHIA COLI APPA2 PHYTASE; PHYTASE; VALINE;

BACTERIUM; HYDROGEN; MUTATION; PROTEIN; SYNERGISM;

AMINO ACID SUBSTITUTION; ARTICLE; BETA SHEET; CATALYSIS; ELECTRICITY; ENZYME ACTIVITY; ENZYME ENGINEERING; ENZYME STRUCTURE; ESCHERICHIA COLI; HIGH TEMPERATURE; HYDROGEN BOND; MELTING POINT; MOLECULAR INTERACTION; MUTATIONAL ANALYSIS; PREDICTION; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; THERMOSTABILITY; WILD TYPE;

6-PHYTASE; ACID PHOSPHATASE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEAT; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; MULTIENZYME COMPLEXES; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN CONFORMATION; PROTEIN ENGINEERING;

ESCHERICHIA COLI;

EID: 46549087211     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-008-1478-2     Document Type: Article

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