Purification and characterization of a novel aminoacylase from Streptomyces mobaraensis

被引:14
作者
Koreishi, M
Asayama, F
Imanaka, H
Imamura, K
Kadota, M
Tsuno, T
Nakanishi, K
机构
[1] Okayama Univ, Fac Engn, Dept Biosci & Biotechnol, Okayama 7008530, Japan
[2] Tsuno Food Ind Co Ltd, Wakayama 6497194, Japan
关键词
aminoacylase; Streptomyces mobaraensis; N-acetyl-L-amino acid; ferulic acid;
D O I
10.1271/bbb.69.1914
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A novel aminoacylase was purified to homogeneity from culture broth of Streptomyces mobaraensis, as evidenced by SDS-polyacrylamide gel electrophoresis (PAGE). The enzyme was a monomer with an approximate molecular mass of 100 kDa. The purified enzyme was inhibited by the presence of 1,10-phenanthroline and activated by the addition of Co2+. It was stable at temperatures of up to 60 degrees C for 1 h at pH 7.2. It showed broad substrate specificity to N-acetylated L-amino acids. It catalyzed the hydrolysis of the amide bonds of various N-acetylated L-amino acids, except for N epsilon-acetyl-L-lysine and N-acetyl-L-proline. Hydrolysis of N-acetyl-L-methionine and N-acetyl-L-histidine followed Michaelis-Menten kinetics with K-m values of 1.3 +/- 0.1 mm and 2.7 +/- 0.1 mm respectively. The enzyme also catalyzed the deacetylation of 7-aminocephalosporanic acid (7-ACA) and cephalosporin C. Moreover, feruloyl-amino acids and L-lysine derivatives of ferulic acid derivatives were synthesized in an aqueous buffer using the enzyme.
引用
收藏
页码:1914 / 1922
页数:9
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