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

  • Kito M
  • Onji Y
  • Yoshida T
  • et al.
FEMS Microbiology Letters (2002) 207(2) 147-151
DOI: 10.1111/j.1574-6968.2002.tb11043.x
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Abstract

O-Poly-L-lysine (O-PL)-degrading enzyme was found in the O-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 O-PL and released L-lysine. The enzyme was a Co 2‡ or Ca 2‡ ion-activated aminopeptidase. ß

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APA

Kito, M., Onji, Y., Yoshida, T., & Nagasawa, T. (2002). Occurrence of ϵ-poly-l-lysine-degrading enzyme in ϵ-poly-l-lysine-tolerant Sphingobacterium multivorum OJ10: purification and characterization. FEMS Microbiology Letters, 207(2), 147–151. https://doi.org/10.1111/j.1574-6968.2002.tb11043.x

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