Characterization of Aspergillus oryzae aspartyl aminopeptidase expressed in Escherichia coli.

Article Details

Citation

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
DrugTargetKindOrganismPharmacological ActionActions
Glutamic acidAspartyl aminopeptidaseProteinHumans
Unknown
Not AvailableDetails