A thermostable variant of fructose bisphosphate aldolase constructed by directed evolution also shows increased stability in organic solvents

Protein Engineering, Design and Selection

Volumn 17, Issue 9, 2004, Pages 689-697

  Hao, Jijun ^a   Berry, Alan ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

Aldolase; Directed evolution; Solvent stability; Thermostability

Indexed keywords

ESCHERICHIA COLI; GENES; MUTAGENESIS; ORGANIC SOLVENTS;

EDWARDSIELLA ICTALURI; FRUCTOSE BISPHOSPHATE ALDOLASE; MUTATIONS; THERMOSTABILITY;

ENZYME INHIBITION;

FRUCTOSE BISPHOSPHATE ALDOLASE; ORGANIC SOLVENT;

ARTICLE; BACTERIAL GENE; CATALYSIS; DNA SEQUENCE; DNA SHUFFLING; EDWARDSIELLA ICTALURI; ENZYME ACTIVITY; ENZYME ISOLATION; ESCHERICHIA COLI; FDA GENE; MOLECULAR EVOLUTION; MOLECULAR STABILITY; MUTATION; PRIORITY JOURNAL; THERMOSTABILITY; WILD TYPE;

ACETONITRILES; AMINO ACID SEQUENCE; DIMETHYLFORMAMIDE; DIRECTED MOLECULAR EVOLUTION; EDWARDSIELLA ICTALURI; ENZYME STABILITY; ESCHERICHIA COLI; FRUCTOSE-BISPHOSPHATE ALDOLASE; HEAT; KINETICS; METHANOL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SOLVENTS; THERMUS;

EDWARDSIELLA ICTALURI; ESCHERICHIA COLI;

EID: 18044366809     PISSN: 17410126     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/gzh081     Document Type: Article

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