Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Microbiology & Fermentation Technology Regular Paper
Purification and Characterization of a Novel Aminoacylase from Streptomyces mobaraensis
Mayuko KOREISHIFumiaki ASAYAMAHiroyuki IMANAKAKoreyoshi IMAMURAMegumi KADOTATakuo TSUNOKazuhiro NAKANISHI
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2005 Volume 69 Issue 10 Pages 1914-1922

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Abstract

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 °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 Nε-acetyl-L-lysine and N-acetyl-L-proline. Hydrolysis of N-acetyl-L-methionine and N-acetyl-L-histidine followed Michaelis–Menten kinetics with Km 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, feruloylamino acids and L-lysine derivatives of ferulic acid derivatives were synthesized in an aqueous buffer using the enzyme.

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© 2005 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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