Characterization of Aspergillus oryzae aspartyl aminopeptidase expressed in Escherichia coli.
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Watanabe J, Tanaka H, Akagawa T, Mogi Y, Yamazaki T
Characterization of Aspergillus oryzae aspartyl aminopeptidase expressed in Escherichia coli.
Biosci Biotechnol Biochem. 2007 Oct;71(10):2557-60. Epub 2007 Oct 7.
- PubMed ID
- 17928682 [ View in PubMed]
- 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.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Glutamic acid Aspartyl aminopeptidase Protein Humans UnknownNot Available Details