A novel ε-lysine acylase (N6-acyl-L-lysine amidohydrolase; EC 220.127.116.11) 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.
|ジャーナル||JAOCS, Journal of the American Oil Chemists' Society|
|出版ステータス||Published - 2005|
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