Purification and Properties of a New Type of Protease Produced by Microbacterium liquefaciens
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概要
- 論文の詳細を見る
A bacterium, identified as Microbacterium liquefaciens MIM-CG-9535-I, was isolated from a soil sample taken from the industrial site of a gelatin manufacturer. A new type of protease, which restrictively decomposes gelatin at one or two positions, was purified from the bacterial culture. The molecular mass of the purified enzyme was 21 kDa by SDS–polyacrylamide gel electrophoresis. The purified enzyme specifically degraded the α-chain of gelatin with a molecular weight of 100 kDa into two peptides of 60 kDa and 40 kDa. Native collagen was not a substrate for the enzyme.
- 社団法人 日本農芸化学会の論文
- 2005-05-23
著者
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Sakai Yasuo
Central Res. Inst. Jellice Co. Ltd.
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Sakai Yasuo
ゼライス中央研究所
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KANAYAMA Yoshitaka
Central Research Institute, Jellice Co., Ltd.
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Kanayama Yoshitaka
Central Research Institute Jellice Co. Ltd.
関連論文
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- Purification and Properties of a New Type of Protease Produced by Microbacterium liquefaciens
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- Development of Low Endotoxin Gelatin for Regenerative Medicine(Biochemistry)
- Promotion by Collagen Tripeptide of Type I Collagen Gene Expression in Human Osteoblastic Cells and Fracture Healing of Rat Femur