Kanayama Yoshitaka, Sakai Yasuo
Central Research Institute, Jellice Co., Ltd., Miyagi, Japan.
Biosci Biotechnol Biochem. 2005 May;69(5):916-21. doi: 10.1271/bbb.69.916.
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 alpha-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.
从一家明胶制造商的工业场地采集的土壤样本中分离出一种细菌，鉴定为液化微杆菌MIM-CG-9535-I。从该细菌培养物中纯化出一种新型蛋白酶，该酶在一个或两个位置限制性地分解明胶。通过SDS-聚丙烯酰胺凝胶电泳测定，纯化酶的分子量为21 kDa。纯化酶将分子量为100 kDa的明胶α链特异性降解为60 kDa和40 kDa的两种肽段。天然胶原蛋白不是该酶的底物。
