Functional expression of a plant hydroxynitrile lyase in Escherichia coli by directed evolution: Creation and characterization of highly in vivo soluble mutants

Protein Engineering, Design and Selection

Volumn 24, Issue 8, 2011, Pages 607-616

  Asano, Yasuhisa ^a   Dadashipour, Mohammad ^a   Yamazaki, Mizue ^a   Doi, Nobutaka ^a   Komeda, Hidenobu ^a  

^a TOYAMA PREFECTURAL UNIVERSITY   (Japan)

Author keywords

directed evolution; functional expression; hydroxynitrile lyase; mutagenesis; protein engineering; protein solubility

Indexed keywords

DIRECTED EVOLUTION; FUNCTIONAL EXPRESSION; HYDROXYNITRILE LYASES; PROTEIN ENGINEERING; PROTEIN SOLUBILITY;

ALDEHYDES; AMINO ACIDS; BIOCHEMICAL ENGINEERING; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; ENZYMES; ESCHERICHIA COLI; GENETIC ENGINEERING; HYDROPHOBICITY; INFRARED SPECTROSCOPY; MUTAGENESIS; SOLUBILITY;

PROTEINS;

HISTIDINE; HYDROXYNITRILE LYASE;

ARTICLE; ENZYME STRUCTURE; ESCHERICHIA COLI; EXPRESSION VECTOR; IN VIVO STUDY; MUTAGENESIS; NONHUMAN; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN ENGINEERING; PROTEIN EXPRESSION; TEMPERATURE MEASUREMENT;

ALDEHYDE-LYASES; AMINO ACID SEQUENCE; CIRCULAR DICHROISM; DIRECTED MOLECULAR EVOLUTION; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; MANIHOT; MOLECULAR SEQUENCE DATA; MUTATION; PLANT PROTEINS; PROTEIN ENGINEERING; PROTEIN STABILITY; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SOLUBILITY; SPECTROMETRY, FLUORESCENCE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE;

ESCHERICHIA COLI;

EID: 79960321967     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzr030     Document Type: Article

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