Purification and characterization of a novel aminoacylase from Streptomyces mobaraensis

Mayuko Koreishi, Fumiaki Asayama, Hiroyuki Imanaka, Koreyoshi Imamura, Megumi Kadota, Takuo Tsuno, Kazuhiro Nakanishi

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


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, feruloyl-amino acids and L-lysine derivatives of ferulic acid derivatives were synthesized in an aqueous buffer using the enzyme.

Original languageEnglish
Pages (from-to)1914-1922
Number of pages9
JournalBioscience, Biotechnology and Biochemistry
Issue number10
Publication statusPublished - Oct 23 2005


  • Aminoacylase
  • Ferulic acid
  • N-acetyl-L-amino acid
  • Streptomyces mobaraensis

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry


Dive into the research topics of 'Purification and characterization of a novel aminoacylase from Streptomyces mobaraensis'. Together they form a unique fingerprint.

Cite this