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Osamu HIRUTA
Department Kumamoto Health Science University , Kumamoto Health Science University Graduate School Division of Health Sciences, Graduate School of Health Sciences Position |
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| Language | English |
| Publication Date | 1993/12 |
| Type | |
| Peer Review | Peer reviewed |
| Title | Purification and Characterization of Poly(γ-glutamic acid) Hydrolase from a Filamentous Fungus, Myrothecium sp. TM-4222 |
| Contribution Type | |
| Journal | Bioscience, Biotechnology, and Biochemistry |
| Journal Type | Japan |
| Volume, Issue, Page | 57(12),pp.2148-2153 |
| Author and coauthor | Toshio Tanaka, Osamu Hiruta, Takafumi Futamura, Kazumichi Uotani, Atsuyuki Satoh, Makoto Taniguchi & Oi Susumu. |
| Details | 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. |