title: Purification and characterization of an epsilon-poly-L-lysine-degrading enzyme from the epsilon-poly-L-lysine-tolerant Chryseobacterium sp. OJ7.
abstract: The epsilon-poly-L-lysine-degrading enzyme of the epsilon-poly-L-lysine-tolerant Chryseobacterium sp. OJ7 was purified and characterized. The bacterium excreted the enzyme into the culture filtrate. The purified enzyme has a molecular mass of approximately 38.4 kDa and consists of two identical subunits with a molecular mass of 19.5 kDa. The enzyme catalyzed the endo-type degradation of epsilon-poly-L-lysine. A correlation between the epsilon-poly-L-lysine tolerance of the bacterium and the high epsilon-poly-L-lysine-degrading activity was suggested.
authors.affiliation: Department of Biomolecular Science, Gifu University, Yanagido, Gifu 501-1193, Japan.
authors.forename: Mitsuaki
authors.initials: M
authors.lastname: Kito
authors.forename: Rika
authors.initials: R
authors.lastname: Takimoto
authors.forename: Yuichi
authors.initials: Y
authors.lastname: Onji
authors.forename: Toyokazu
authors.initials: T
authors.lastname: Yoshida
authors.forename: Toru
authors.initials: T
authors.lastname: Nagasawa