Pyranose 2-oxidase from Phanerochaete chrysosporium-Expression in E. coli and biochemical characterization

Journal of Biotechnology

Volumn 142, Issue 2, 2009, Pages 97-106

  Pisanelli, Ines ^a   Kujawa, Magdalena ^a,d   Spadiut, Oliver ^a   Kittl, Roman ^a,d   Halada, Petr ^b   Volc, Jindrich ^b   Mozuch, Michael D ^c   Kersten, Philip ^c   Haltrich, Dietmar ^a   Peterbauer, Clemens ^a  

^a UNIVERSITY OF NATURAL RESOURCES AND LIFE SCIENCES   (Austria)

^b INSTITUTE OF MICROBIOLOGY   (Czech Republic)

^c FOREST PRODUCTS LABORATORY   (United States)

^d RESEARCH CENTRE APPLIED BIOCATALYSIS   (Austria)

Author keywords

Heterologous expression; Lignocellulose degradation; Phanerochaete chrysosporium; Pyranose 2 oxidase

Indexed keywords

BENZOQUINONE; BIOCHEMICAL CHARACTERIZATION; CATALYTIC EFFICIENCIES; CATALYTIC PROPERTIES; CHRYSOSPORIUM; DICHLOROINDOPHENOL; E. COLI; ELECTRON ACCEPTOR; ELECTRON DONORS; ENZYME PREPARATION; EXPRESSION VECTORS; FERRICENIUM; HETEROLOGOUS EXPRESSION; IN-VIVO; LIGNOCELLULOSE DEGRADATION; N-TERMINAL; ONE-STEP PURIFICATION; PHANEROCHAETE CHRYSOSPORIUM; PYRANOSE; PYRANOSE 2-OXIDASE; RECOMBINANT ENZYMES; SPECIFIC ACTIVITY;

CELLULOSE; DEGRADATION; ENZYMES; ESCHERICHIA COLI; LIGNIN; OXYGEN; SUBSTRATES; SUGAR (SUCROSE); SUGARS;

GENE ENCODING;

OXIDOREDUCTASE; PYRANOSE 2 OXIDASE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; FUNGAL GENE; GENE ISOLATION; HETEROLOGOUS EXPRESSION; NONHUMAN; NUCLEOTIDE SEQUENCE; PHANEROCHAETE; PRIORITY JOURNAL; PROTEIN FUNCTION;

AMINO ACID SEQUENCE; BENZOQUINONES; CARBOHYDRATE DEHYDROGENASES; CHROMATOGRAPHY, AFFINITY; ELECTROPHORESIS; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; KINETICS; LIGNIN; MOLECULAR SEQUENCE DATA; PHANEROCHAETE; RECOMBINANT PROTEINS; SEQUENCE ANALYSIS, PROTEIN;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PHANEROCHAETE CHRYSOSPORIUM;

EID: 67349210370     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2009.03.019     Document Type: Article

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