Characterization of an Aspergillus oryzae cysteinyl dipeptidase expressed in Escherichia coli

Ref ID: 18385

Author:

Ryota Hattori , Mayumi Matsusita-Morita , Sawaki
Tada , Junichiro Marui , Ikuyo Furukawa , Satoshi Suzuki , Hitoshi Amano , Hiroki Ishida , Youhei Yamagata , Michio Takeuchi , Ken-Ichi Kusumoto

Author address:

National Food Research Institute, Ibaraki, Japan, Amano Enzyme Inc., Gifu, Japan, Gekkeikan Sake Company Ltd., Kyoto, Japan, Tokyo University
of Agriculture and Technology, Tokyo, Japan

Full conference title:

Asperfest 8

Abstract:

Cysteinyl dipeptidase from A. oryzae (CdpA) was produced in Escherichia coli and purified. CdpA formed a homodimer and its molecular mass was
determined as 109 kDa. CdpA-specific activity to Cys-Gly was 3.04 U/mg. The enzyme showed maximum hydrolyzing activity toward Ala-Cys, followed
by Leu-Cys, Cys-Gly, Cys-Ala, and Gly-Cys among the cysteine-containing dipeptide substrates. Its substrate specificity was distinct from those of other
cysteinyl dipeptidases of the M20 family. The activity of CdpA was increased by addition of Mn , Zn , and Co at 0.1 mM. The activity was inhibited
2+ 2+ 2+
in the presence of Fe . Several protease inhibitors reduced the activity. The complete inhibition of enzyme activity by EDTA indicates that CdpA is a
2+
metallopeptidase. It was optimally active at pH 7-8 and stable at pH 6-9 and at up to 40 . This study was supported by the Program for Promotion of Basic
Research Activities for Innovative Biosciences (PROBRAIN).

Abstract Number: 63)

Conference Year: 2011

Link to conference website: NULL

New link: NULL

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