Direct over-expression, characterization and H2O2 stability study of active Pleurotus eryngii versatile peroxidase in Escherichia coli

Biotechnology Letters

Volumn 34, Issue 8, 2012, Pages 1537-1543

  Bao, Xue ^a,b   Liu, Aiqiu ^a,b   Lu, Xuefeng ^a   Li, Jian Jun ^a  

^a QINGDAO INSTITUTE OF BIOENERGY AND BIOPROCESS TECHNOLOGY   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

Escherichia coli; Hydrogen peroxide stability; Overexpression; Peroxidase; Pleurotus eryngii

Indexed keywords

CODON OPTIMIZATION; E. COLI; FUSION PROTEINS; NICKEL COLUMN; OVER-EXPRESSION; PEROXIDASE; PLEUROTUS ERYNGII; REACTIVE BLACK 5; RZ VALUE; STABILITY STUDY; VERATRYL ALCOHOL; VERSATILE PEROXIDASE;

CLONING; ENZYME ACTIVITY; GENE ENCODING; HYDROGEN PEROXIDE; MANGANESE; MANGANESE COMPOUNDS; PURIFICATION;

ESCHERICHIA COLI;

FUNGAL PROTEIN; HYDROGEN PEROXIDE; PEROXIDASE; RECOMBINANT PROTEIN;

ARTICLE; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; METABOLISM; PLEUROTUS;

ENZYME STABILITY; ESCHERICHIA COLI; FUNGAL PROTEINS; HYDROGEN PEROXIDE; PEROXIDASES; PLEUROTUS; RECOMBINANT PROTEINS;

ANIMALIA; ESCHERICHIA COLI; PLEUROTUS ERYNGII;

EID: 84864387203     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-012-0940-5     Document Type: Article

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