ゲノム情報を利用した麹菌タンパク質分解酵素を中心とした応用と開発

メンバー: 山形洋平
分野: 農芸化学、生物科学、外科系臨床医学
所属: 農学研究院
キーワード: Aspergillus oryzae、 protease、 peptidase、 Aspergilli、 mirobial protease
ウェブサイト:
研究概要

麹菌は、酒、味噌、醤油など伝統的な発酵食品、いわゆるスローフードを生産する際に用いられている日本を代表する微生物です。食品ばかりでなく、異種タンパク質生産や医薬品生産にも重要な役割を果たしています。また、私たちの研究室を含む All Japan Team によって世界で初めて全ゲノム解析が終了した糸状菌(カビ)の一つでもあります。私達は、ゲノムデータベース中から約130種のタンパク質分解酵素遺伝子を見出しています。この数は、同時期に解析された Aspergillus fumigatus や A. nidulans の遺伝子中に存在するタンパク質分解酵素遺伝子数に比べて約1.3倍程度多いものでした。この多数の酵素を持つ理由を明らかにするためにこれらの酵素の様々な性質を明らかにしています。
主要論文・参考事項
K Ishida, M Kuboshima, H Morita, H Maeda, A Okamoto, M Takeuchi & Y Yamagata, (2014) Diversity in mRNA expression of the serine-type carboxypeptidase ocpG in Aspergillus oryzae through intron retention. Biosc Biotech Biochem, 78,1328-1336.
M Matsushita-Morita, H Nakagawa, S Tada, J Marui, H Hattori, S Suzuki, Y Yamagata, H Amano, H Ishida, M Takeuchi & K-I, Kusumoto (2013) Characterization of a (D)-stereo-selective aminopeptidase (DamA) exhibiting aminolytic activity and halophilicity from Aspergillus oryzae. Appl Biochem Biotechnol, 171, 145-164
H Morita, S Tomita, H Maeda, A Okamoto, Y Yamagata, K-I Kusumoto, H Amano, H Ishida, M Takeuchi (2012) A serine-type carboxypeptidase KexA of Aspergillus oryzae has broader substrate specificity than yeast Kex1, and is required for normal hyphal growth and conidiation. Appl Environ Microbiol, 78, 8154-8157
Marui J, Matsushita-Morita M, Tada S, Hattori R, Suzuki S, Amano H, Ishida H, Yamagata Y, Takeuchi M, Kusumoto K-I, Comparison of expression and enzymatic properties of Aspergillus oryzae lysine aminopeptidase ApsA and ApsB. World J Microbiol Biotechnol, 28, 2643-2650 (2012)
H Morita, H Abo, A Okamoto, H Maeda, Y Yamagata, K-I Kusumoto, H Amano, H Ishida, M Takeuchi, Enzymatic properties of the recombinant serine-type carboxypeptidase OcpC, which is unique to Aspergillus oryzae. Biosci Biotechnol Biochem, 75, 662-668 (2011)
お問い合わせ先
東京農工大学・先端産学連携研究推進センター
urac[at]ml.tuat.ac.jp([at]を@に変換してください)
Application and development of proteolytic enzymes from Aspergilli

Research members: Youhei Yamagata PhD.
Research fields: Agricultural chemistry, Biological Science, Clinical surgery
Departments: Institute of Agriculture
Keywords: Aspergillus oryzae, protease, peptidase, Aspergilli, mirobial protease
Web site:
Summary

Aspergillus oryzae (A. oryzae) has been used in the production of traditional Japanese fermented foods and beverages for more than a thousand years. The fungus is classified as GRAS grade by the FDA. It is also known that the fungus is able to release a variety of extracellular enzymes, which are used by the host organism for recombinant protein production. A widely used fungus, A. oryzae is one of the first fungi with a whole genome sequence that was determined in 2005, and we reported that the 134 proteolytic enzyme should be encoded in A. oryzae genome by ORF search and its annotation in the report.
The number of the deduced proteolytic enzymes encoded in the A. oryzae genome is >1.3 times higher than other Aspergillus species, whose genome sequences were concurrently reported, (such as A. nidulans and A. fumigatus). It was postulated that A. oryzae acquired the odd proteolytic enzymes by horizontal gene transfer. However, the reason behind the maintenance of these additional genes has been not clear. Hence, in this study, we tried to shed light on the role of each proteolytic enzyme through its profiling. The study is based on our hypothesis that enzymes with different functional roles also display different profiles (for e.g., substrate specificity)
Reference articles and patents
K Ishida, M Kuboshima, H Morita, H Maeda, A Okamoto, M Takeuchi & Y Yamagata, (2014) Diversity in mRNA expression of the serine-type carboxypeptidase ocpG in Aspergillus oryzae through intron retention. Biosc Biotech Biochem, 78,1328-1336.
M Matsushita-Morita, H Nakagawa, S Tada, J Marui, H Hattori, S Suzuki, Y Yamagata, H Amano, H Ishida, M Takeuchi & K-I, Kusumoto (2013) Characterization of a (D)-stereo-selective aminopeptidase (DamA) exhibiting aminolytic activity and halophilicity from Aspergillus oryzae. Appl Biochem Biotechnol, 171, 145-164
H Morita, S Tomita, H Maeda, A Okamoto, Y Yamagata, K-I Kusumoto, H Amano, H Ishida, M Takeuchi (2012) A serine-type carboxypeptidase KexA of Aspergillus oryzae has broader substrate specificity than yeast Kex1, and is required for normal hyphal growth and conidiation. Appl Environ Microbiol, 78, 8154-8157
Marui J, Matsushita-Morita M, Tada S, Hattori R, Suzuki S, Amano H, Ishida H, Yamagata Y, Takeuchi M, Kusumoto K-I, Comparison of expression and enzymatic properties of Aspergillus oryzae lysine aminopeptidase ApsA and ApsB. World J Microbiol Biotechnol, 28, 2643-2650 (2012)
H Morita, H Abo, A Okamoto, H Maeda, Y Yamagata, K-I Kusumoto, H Amano, H Ishida, M Takeuchi, Enzymatic properties of the recombinant serine-type carboxypeptidase OcpC, which is unique to Aspergillus oryzae. Biosci Biotechnol Biochem, 75, 662-668 (2011)
Contact
University Research Administration Center(URAC),
Tokyo University of Agriculture andTechnology
urac[at]ml.tuat.ac.jp
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