A novel ε-lysine acylase from Streptomyces mobaraensis for synthesis of Nε-acyl-L-lysines

Mayuko Koreishi, Ryoko Kawasaki, Hiroyuki Imanaka, Koreyoshi Imamura, Kazuhiro Nakanishi

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

A novel ε-lysine acylase (N6-acyl-L-lysine amidohydrolase; EC 3.5.1.17) was isolated from Streptomyces mobaraensis and purified to homogeneity by SDS-PAGE from the culture broth. The purified enzyme was monomeric, with a molecular mass of approximately 60 kDa. The enzyme was inactivated by the presence of 1, 10-phenanthroline and activated in the presence of Co2+ and Zn2+. The enzyme showed a pH optimum of 8.0 and was stable at temperatures of up to 50°C for 1 h at pH 8.0. The enzyme specifically catalyzed the hydrolysis of the amide bond of various Nε-acyl-L-lysines. Furthermore, the enzyme efficiently catalyzed the synthesis of Nε-acyl-L-lysines with fatty and aromatic acyl groups in an aqueous buffer. In the syntheses of Nε-decanoyl-L-lysine, Nε-lauroyl-L-lysine, and Nε-myristoyl-L-lysine, the product precipitated and the yield was 90% or higher using 10 mM FA and 0.5 M L-lysine as the substrate.

Original languageEnglish
Pages (from-to)631-637
Number of pages7
JournalJAOCS, Journal of the American Oil Chemists' Society
Volume82
Issue number9
DOIs
Publication statusPublished - Dec 1 2005

Keywords

  • Enzymatic synthesis
  • Nε-acyl-l-lysine
  • Nε-lauroyl-L-lysine
  • Streptomyces mobaraensis
  • ε-lysine acylase

ASJC Scopus subject areas

  • Chemical Engineering(all)
  • Organic Chemistry

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