耐ε-聚-L-赖氨酸的多食鞘氨醇杆菌OJ10中ε-聚-L-赖氨酸降解酶的产生：纯化与特性分析
Occurrence of epsilon-poly-L-lysine-degrading enzyme in epsilon-poly-L-lysine-tolerant Sphingobacterium multivorum OJ10: purification and characterization.
作者信息
Kito Mitsuaki, Onji Yuichi, Yoshida Toyokazu, Nagasawa Toru
机构信息
Department of Biomolecular Science, Faculty of Engineering, Gifu University, Yanagido, 501-1193, Gifu, Japan.
出版信息
FEMS Microbiol Lett. 2002 Feb 5;207(2):147-51. doi: 10.1111/j.1574-6968.2002.tb11043.x.
Abstract
Epsilon-poly-L-lysine (epsilon-PL)-degrading enzyme was found in the epsilon-PL-tolerant strain Sphingobacterium multivorum OJ10 and purified to homogeneity. The purified enzyme has a molecular mass of approximately 80 kDa. The enzyme catalyzed exo-type degradation of epsilon-PL and released L-lysine. The enzyme was a Co2+ or Ca2+ ion-activated aminopeptidase.
摘要
在耐ε-聚-L-赖氨酸（ε-PL）的多食鞘氨醇杆菌OJ10中发现了ε-聚-L-赖氨酸降解酶，并将其纯化至同质。纯化后的酶分子量约为80 kDa。该酶催化ε-PL的外切型降解并释放出L-赖氨酸。该酶是一种Co2+或Ca2+离子激活的氨肽酶。
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