title: Characterization of Aspergillus oryzae aspartyl aminopeptidase expressed in Escherichia coli.
abstract: To characterize aspartyl aminopeptidase from Aspergillus oryzae, the recombinant enzyme was expressed in Escherichia coli. The enzyme cleaves N-terminal acidic amino acids. About 30% activity was retained in 20% NaCl. Digestion of defatted soybean by the enzyme resulted in an increase in the glutamic acid content, suggesting that the enzyme is potentially responsible for the release of glutamic acid in soy sauce mash.
authors.affiliation: Manufacturing Division, Yamasa Shoyu Corporation, Japan. j.watanabe@yamasa.com
authors.forename: Jun
authors.initials: J
authors.lastname: Watanabe
authors.forename: Hisaki
authors.initials: H
authors.lastname: Tanaka
authors.forename: Takumi
authors.initials: T
authors.lastname: Akagawa
authors.forename: Yoshinobu
authors.initials: Y
authors.lastname: Mogi
authors.forename: Tatsuo
authors.initials: T
authors.lastname: Yamazaki
mesh_terms: D001236:Aspergillus oryzae / Q000201:enzymology*; D002118:Calcium / Q000494:pharmacology; D002614:Chelating Agents / Q000494:pharmacology; D004305:Dose-Response Relationship, Drug; D004492:Edetic Acid / Q000494:pharmacology; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics; D043384:Glutamyl Aminopeptidase / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D010618:Phenanthrolines / Q000494:pharmacology; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D012965:Sodium Chloride / Q000494:pharmacology; D013379:Substrate Specificity; D013696:Temperature; D013997:Time Factors; D015032:Zinc / Q000494:pharmacology
chemical_list: D002614:Chelating Agents; D010618:Phenanthrolines; D011994:Recombinant Proteins; D012965:Sodium Chloride; D004492:Edetic Acid; D043384:Glutamyl Aminopeptidase; D015032:Zinc; D002118:Calcium; C025205:1,10-phenanthroline