Occurrence of ɛ-poly-l-lysine-degrading enzyme in ?-poly-l-lysine-tolerant Sphingobacterium multivorum OJ10: purification and characterization

Occurrence of ɛ-poly-l-lysine-degrading enzyme in ?-poly-l-lysine-tolerant Sphingobacterium multivorum OJ10: purification and characterization

Abstract ɛ-Poly-l-lysine (ɛ-PL)-degrading enzyme was found in the ɛ-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 ɛ-PL and released l-lysine. The enzyme w...

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Veröffentlicht in:FEMS microbiology letters 2002-02, Vol.207 (2), p.147-151
Hauptverfasser: Kito, Mitsuaki, Onji, Yuichi, Yoshida, Toyokazu, Nagasawa, Toru
Format: Artikel
Sprache:eng
Schlagworte:
Aminopeptidase
Calcium
Calcium ions
Carbon dioxide
Cobalt
Degradation
Enzymes
Lysine
Microbiology
Poly-L-lysine
Purification
Sphingobacterium
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Zusammenfassung:Abstract ɛ-Poly-l-lysine (ɛ-PL)-degrading enzyme was found in the ɛ-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 ɛ-PL and released l-lysine. The enzyme was a Co2+ or Ca2+ ion-activated aminopeptidase.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.2002.tb11043.x