A novel non-thermostable deuterolysin from Aspergillus oryzae-Reference-Cited by-同舟云学术

A novel non-thermostable deuterolysin from Aspergillus oryzae

Published:2016-09-01 Issue:9 Volume:80 Page:1813-1819
ISSN:0916-8451
Container-title:Bioscience, Biotechnology, and Biochemistry
language:en
Short-container-title:

Author:

Maeda Hiroshi¹,Katase Toru²³,Sakai Daisuke¹,Takeuchi Michio¹,Kusumoto Ken-Ichi⁴,Amano Hitoshi³,Ishida Hiroki⁵,Abe Keietsu²,Yamagata Youhei¹

Affiliation:

1. Department of Applied Biological Chemistry, The Graduate School of Agriculture, Tokyo University of Agriculture and Technology, Fuchu, Tokyo, Japan

2. Division of Life Science, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan

3. Amano Enzyme Inc, Nagoya, Japan

4. National Food Research Institute, Tsukuba, Japan

5. Gekkeikan Sake Co., Ltd, Fushimi-ku, Kyoto, Japan

Abstract

Abstract Three putative deuterolysin (EC 3.4.24.29) genes (deuA, deuB, and deuC) were found in the Aspergillus oryzae genome database (http://www.bio.nite.go.jp/dogan/project/view/AO). One of these genes, deuA, was corresponding to NpII gene, previously reported. DeuA and DeuB were overexpressed by recombinant A. oryzae and were purified. The degradation profiles against protein substrates of both enzymes were similar, but DeuB showed wider substrate specificity against peptidyl MCA-substrates compared with DeuA. Enzymatic profiles of DeuB except for thermostability also resembled those of DeuA. DeuB was inactivated by heat treatment above 80° C, different from thermostable DeuA. Transcription analysis in wild type A. oryzae showed only deuB was expressed in liquid culture, and the addition of the proteinous substrate upregulated the transcription. Furthermore, the NaNO3 addition seems to eliminate the effect of proteinous substrate for the transcription of deuB.

Funder

PROBRAIN

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

Link

http://academic.oup.com/bbb/article-pdf/80/9/1813/36832691/bbb1813.pdf

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