Purification and characterization of an ε-poly-L-lysine-degrading enzyme from an ε-poly-L-lysine-producing strain of Streptomyces albulus

@article{Kito2002PurificationAC,
  title={Purification and characterization of an ε-poly-L-lysine-degrading enzyme from an ε-poly-L-lysine-producing strain of Streptomyces albulus},
  author={Mitsuaki Kito and Rika Takimoto and Toyokazu Yoshida and Toru Nagasawa},
  journal={Archives of Microbiology},
  year={2002},
  volume={178},
  pages={325-330}
}
An ε-poly-L-lysine-degrading enzyme of an ε-poly-L-lysine-producing strain of Streptomyces albulus was purified and characterized. The enzyme was tightly bound to the cell membrane. After solubilization with NaSCN, the enzyme was purified to homogeneity by phenyl-Sepharose CL-4B column chromatography. The subunit molecular mass of the purified enzyme was 54 kDa. Enzyme activity was inhibited by o-phenanthroline, and could be restored in the presence of 1 mM Mg2+, Ca2+, Fe3+ or Zn2+. The mode of… CONTINUE READING
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Improved ε-poly-L-lysine production of an S-(2-aminoethyl)-L-cysteine resistant mutant of Streptomyces albulus

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