Characterization of Aspergillus oryzae aspartyl aminopeptidase expressed in Escherichia coli
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Inhibition of Aspergillus flavus Growth and Aflatoxin Production in Transgenic Maize Expressing the α-amylase Inhibitor from Lablab purpureus L.
Published on: February 15, 2019
Jun Watanabe1, Hisaki Tanaka, Takumi Akagawa
1Manufacturing Division, Yamasa Shoyu Corporation, Japan. j.watanabe@yamasa.com
Bioscience, Biotechnology, and Biochemistry
|October 12, 2007
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.
