A single residual replacement improves the folding and stability of recombinant cassava hydroxynitrile lyase in E. coli

Biotechnology Letters

Volumn 25, Issue 13, 2003, Pages 1041-1047

  Yan, Gonghong ^a   Cheng, Shuhua ^b   Zhao, Guogang ^a   Wu, Sheng ^a   Liu, Yanbing ^a   Sun, Wanru ^a  

^a INSTITUTE OF MICROBIOLOGY   (China)

^b WEILL CORNELL MEDICAL COLLEGE   (United States)

Author keywords

hydroxynitrile lyase; Cassava; Enzyme stability; Site directed mutagenesis

Indexed keywords

ACETONITRILE DERIVATIVE; HYDROXYMANDELONITRILE LYASE; LYASE; MANDELONITRILE; RECOMBINANT PROTEIN;

ARTICLE; CASSAVA; CHEMISTRY; CIRCULAR DICHROISM; ENZYME ACTIVATION; ENZYME STABILITY; ENZYMOLOGY; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; METHODOLOGY; MOLECULAR WEIGHT; MUTATION; PH; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; TEMPERATURE;

ACETONITRILES; ALDEHYDE-LYASES; CIRCULAR DICHROISM; ENZYME ACTIVATION; ENZYME STABILITY; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, ENZYMOLOGIC; HYDROGEN-ION CONCENTRATION; MANIHOT; MOLECULAR WEIGHT; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPERATURE;

ESCHERICHIA COLI; MANIHOT; MANIHOT ESCULENTA;

EID: 0042862842     PISSN: 01415492     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1024182228057     Document Type: Article

References (13)

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