Biochemical characterization of Aspergillus oryzae native tannase and the recombinant enzyme expressed in Pichia pastoris

Journal of Bioscience and Bioengineering

Volumn 118, Issue 4, 2014, Pages 392-395

  Mizuno, Toshiyuki ^a   Shiono, Yoshihito ^a   Koseki, Takuya ^a  

^a YAMAGATA UNIVERSITY   (Japan)

Author keywords

Aspergillus oryzae; Esterase; Substrate specificity; Tannase

Indexed keywords

ASPERGILLUS; ELECTROPHORESIS; ESTERIFICATION; ESTERS; FLAVONOIDS; MOLECULAR MASS; PARABENS; PURIFICATION; RECOMBINANT PROTEINS; SODIUM DODECYL SULFATE; SODIUM SULFATE; SUBSTRATES; YEAST;

ASPERGILLUS ORYZAE; BIOCHEMICAL CHARACTERIZATION; BIOCHEMICAL PROPERTIES; CATALYTIC EFFICIENCIES; ESTERASE; SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS; SUBSTRATE SPECIFICITY; TANNASE;

ENZYMES;

4 HYDROXYBENZOIC ACID; CAFFEIC ACID; CATECHIN; EPICATECHIN; EPIGALLOCATECHIN GALLATE; ESTERASE; FERULIC ACID; FERULOYL ESTERASE; FUNGAL ENZYME; GALLIC ACID METHYL ESTER; GALLIC ACID PROPYL ESTER; HYDROLASE; PARA COUMARIC ACID; PARABEN HYDROLASE; RECOMBINANT ENZYME; RECOMBINANT TANNASE; SINAPIC ACID; TANNASE; UNCLASSIFIED DRUG; CARBOXYLESTERASE; FUNGAL PROTEIN; PROTEIN SUBUNIT; RECOMBINANT PROTEIN;

ARTICLE; ASPERGILLUS ORYZAE; BIOCHEMICAL COMPOSITION; CONTROLLED STUDY; DEGLYCOSYLATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME STABILITY; ENZYME SUBSTRATE; KOMAGATAELLA PASTORIS; MOLECULAR WEIGHT; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN EXPRESSION; STABLE EXPRESSION; ANALOGS AND DERIVATIVES; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; GENE EXPRESSION; GENETICS; KINETICS; METABOLISM; PH; PICHIA; PROTEIN SUBUNIT;

ASPERGILLUS ORYZAE; PICHIA PASTORIS;

ASPERGILLUS ORYZAE; CARBOXYLIC ESTER HYDROLASES; CATECHIN; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FUNGAL PROTEINS; GENE EXPRESSION; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR WEIGHT; PICHIA; PROTEIN SUBUNITS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

EID: 84921635058     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2014.04.003     Document Type: Article

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