Production of soluble recombinant proteins in Escherichia coli: Effects of process conditions and chaperone co-expression on cell growth and production of xylanase

Bioresource Technology

Volumn 123, Issue , 2012, Pages 135-143

  Jhamb, Kamna ^a   Sahoo, Debendra K ^a  

^a INSTITUTE OF MICROBIAL TECHNOLOGY   (India)

Author keywords

Escherichia coli; Inclusion bodies; Molecular chaperones; Soluble expression

Indexed keywords

CHAPERONE CO-EXPRESSION; CO-EXPRESSION; EFFECTS OF TEMPERATURE; INCLUSION BODIES; MODEL PROTEINS; MOLECULAR CHAPERONES; PROCESS CONDITION; SOLUBLE ENZYMES; SOLUBLE EXPRESSION; SOLUBLE FRACTION; TARGET PROTEINS; XYLANASES;

CELL GROWTH; GROWTH KINETICS; RECOMBINANT PROTEINS;

ESCHERICHIA COLI;

CHAPERONE; CHAPERONIN; PROTEIN DNAE; PROTEIN DNAJ; PROTEIN DNAK; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; XYLAN ENDO 1,3 BETA XYLOSIDASE;

BIOLOGICAL PRODUCTION; CELL ORGANELLE; COLIFORM BACTERIUM; CONCENTRATION (COMPOSITION); ENZYME ACTIVITY; GENE EXPRESSION; MOLECULAR ANALYSIS; PROTEIN; RECOMBINATION; SOLUBILIZATION;

ARTICLE; CELL GROWTH; CULTURE MEDIUM; ENZYME INDUCTION; ENZYME SYNTHESIS; ESCHERICHIA COLI; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; SOLUBILITY; TEMPERATURE SENSITIVITY;

BIOTECHNOLOGY; ENDO-1,4-BETA XYLANASES; ESCHERICHIA COLI; ISOPROPYL THIOGALACTOSIDE; MOLECULAR CHAPERONES; RECOMBINANT PROTEINS; SOLUBILITY; TEMPERATURE; TIME FACTORS;

ESCHERICHIA COLI;

EID: 84865539975     PISSN: 09608524     EISSN: 18732976     Source Type: Journal    
DOI: 10.1016/j.biortech.2012.07.011     Document Type: Article

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