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A novel ∈‐lysine acylase from Streptomyces mobaraensis for synthesis of N∈ ‐acyl‐ l ‐lysines
Author(s) -
Koreishi Mayuko,
Kawasaki Ryoko,
Imanaka Hiroyuki,
Imamura Koreyoshi,
Nakanishi Kazuhiro
Publication year - 2005
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/s11746-005-1121-2
Subject(s) - lysine , chemistry , enzyme , amidohydrolase , acylation , substrate (aquarium) , hydrolysis , biochemistry , streptomyces , stereochemistry , hydantoin , amino acid , catalysis , biology , bacteria , ecology , genetics
A novel ∈‐lysine acylase ( N 6 ‐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 Co 2+ and Zn 2+ . 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 N ∈‐acyl‐ l ‐lysines. Furthermore, the enzyme efficiently catalyzed the synthesis of N ∈‐acyl‐ l ‐lysines with fatty and aromatic acyl groups in an aqueous buffer. In the syntheses of N ∈‐decanoyl‐ l ‐lysine, N ∈‐lauroyl‐ l ‐lysine, and N ∈‐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.