Enhanced secretory production of hemolysin-mediated cyclodextrin glucanotransferase in Escherichia coli by random mutagenesis of the ABC transporter system

Journal of Biotechnology

Volumn 150, Issue 4, 2010, Pages 453-459

  Low, Kheng Oon ^a   Mahadi, Nor Muhammad ^b   Abdul Rahim, Raha ^c   Rabu, Amir ^b   Abu Bakar, Farah Diba ^b   Abdul Murad, Abdul Munir ^b   Md Illias, Rosli ^a  

^a UNIVERSITI TEKNOLOGI MALAYSIA   (Malaysia)

^b UNIVERSITI KEBANGSAAN MALAYSIA   (Malaysia)

^c UNIVERSITY PUTRA MALAYSIA   (Malaysia)

Author keywords

Alpha hemolysin transport system; Cyclodextrin glucanotransferase; Directed evolution; Escherichia coli; Extracellular secretion

Indexed keywords

ABC TRANSPORTER; CYCLODEXTRIN GLUCANOTRANSFERASE; CYCLODEXTRIN GLUCANOTRANSFERASES; DIRECTED EVOLUTION; E. COLI; ERROR PRONE PCR; EXTRACELLULAR MEDIUM; EXTRACELLULAR SECRETION; MUTATION SITES; PARENT STRAIN; RANDOM MUTAGENESIS; TARGET PROTEINS; TRANS-MEMBRANE DOMAINS; TRANSFORMANTS; TRANSPORT SYSTEMS; WILD-TYPE STRAIN;

ACTIVATION ANALYSIS; AMINO ACIDS; BIOLOGY; BLOOD;

ESCHERICHIA COLI;

ABC TRANSPORTER; ALPHA HEMOLYSIN; BACTERIAL ENZYME; CYCLOMALTODEXTRIN GLUCANOTRANSFERASE; MUTANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME RELEASE; ENZYME SYNTHESIS; ESCHERICHIA COLI; MEMBRANE POTENTIAL; MUTATIONAL ANALYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ENGINEERING; PROTEIN EXPRESSION; PROTEIN VARIANT; SITE DIRECTED MUTAGENESIS; WILD TYPE;

ATP-BINDING CASSETTE TRANSPORTERS; BLOTTING, WESTERN; DIRECTED MOLECULAR EVOLUTION; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GLUCOSYLTRANSFERASES; HEMOLYSIN PROTEINS; MUTAGENESIS; MUTATION, MISSENSE; OLIGONUCLEOTIDES; PLASMIDS; PROTEIN ENGINEERING;

ESCHERICHIA COLI;

EID: 78649443670     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2010.10.001     Document Type: Article

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