Purification and characterization of a glutaminase enzyme accounting for the majority of glutaminase activity in Aspergillus sojae under solid-state culture

Applied Microbiology and Biotechnology

Volumn 97, Issue 19, 2013, Pages 8581-8590

  Ito, Kotaro ^a,b   Hanya, Yoshiki ^b   Koyama, Yasuji ^a  

^a Noda Institute for Scientific Research   (Japan)

^b KIKKOMAN CORPORATION   (Japan)

Author keywords

Aspergillus; Expression; Gene disruption; Glutaminase; Purification

Indexed keywords

AMINO ACIDS; DIMERS; ENZYMES; GEL PERMEATION CHROMATOGRAPHY; GENES; PURIFICATION;

ASPERGILLUS ORYZAE; EXPRESSION; GEL-FILTRATION CHROMATOGRAPHY; GENE DISRUPTIONS; GLUTAMINASE; OPTIMAL TEMPERATURE; SOLID STATE CULTURE; SUBSTRATE SPECIFICITY;

ASPERGILLUS;

ASPARAGINE; GLUTAMINASE; GLUTAMINE;

ENZYME; ENZYME ACTIVITY; FILTRATION; GENE EXPRESSION; GENOME; PH; PROTEIN; PURIFICATION; SUBSTRATE;

ARTICLE; ASPERGILLUS PARASITICUS; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME SPECIFICITY; FUNGAL GENE; GEL FILTRATION CHROMATOGRAPHY; MOLECULAR WEIGHT; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS;

ASPERGILLUS; ASPERGILLUS ORYZAE; ASPERGILLUS SOJAE;

ASPERGILLUS; CHROMATOGRAPHY, GEL; DNA, FUNGAL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME STABILITY; GENE DELETION; GLUTAMINASE; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PHYLOGENY; PROTEIN MULTIMERIZATION; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TEMPERATURE;

EID: 84885379860     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-013-4693-4     Document Type: Article

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