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ヒルタ オサム
Osamu HIRUTA
蛭田 修 所属 熊本保健科学大学 品質保証・精度管理学共同研究講座 熊本保健科学大学大学院 保健科学研究科 保健科学専攻 職位 特命教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 1993/12 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Purification and Characterization of Poly(γ-glutamic acid) Hydrolase from a Filamentous Fungus, Myrothecium sp. TM-4222 |
| 執筆形態 | 共著 |
| 掲載誌名 | Bioscience, Biotechnology, and Biochemistry |
| 掲載区分 | 国内 |
| 巻・号・頁 | 57(12),pp.2148-2153 |
| 著者・共著者 | Toshio Tanaka, Osamu Hiruta, Takafumi Futamura, Kazumichi Uotani, Atsuyuki Satoh, Makoto Taniguchi & Oi Susumu. |
| 概要 | Poly(γ-glutamic acid) (PGA) hydrolase was purified from the culture filtrate of Myrothecium sp. TM-4222 and its general properties, especially the mode of hydrolytic action on the γ-glutamyl bond of PGA, were investigated. The molecular mass was estimated to be 68 kDa by gel filtration. The hydrolytic action of the enzyme was specific for PGA, but not for other γ-glutamyl peptides or amides. The enzyme converted 38% of the original PGA with an average molecular mass of 500 kDa to smaller peptides, and then depolymerized these fragments to a mixture of γ-oligopeptides which consisted of only L-glutamic acid. L-Glutamic acid monomer was negligible in the reaction mixture. The remaining 62% of PGA was resistant to the enzyme action, in which D-glutamic acid was mainly detected. This study demonstrated a novel endo-type specificity of hydrolysis on PGA by the enzyme. |