Purification, Characterization, Molecular Cloning, and Expression of a New Aminoacylase from<i>Streptomyces mobaraensis</i>That Can Hydrolyze<i>N</i>-(Middle/Long)-chain-fatty-acyl-<scp>L</scp>-amino Acids as Well as<i>N</i>-Short-chain-acyl-<scp>L</scp>-amino acids

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  • KOREISHI Mayuko
    Division of Chemistry and Biochemistry, Graduate School of Natural Science and Technology, Okayama University
  • NAKATANI Yasuyuki
    Division of Chemistry and Biochemistry, Graduate School of Natural Science and Technology, Okayama University
  • OOI Manami
    Division of Chemistry and Biochemistry, Graduate School of Natural Science and Technology, Okayama University
  • IMANAKA Hiroyuki
    Division of Chemistry and Biochemistry, Graduate School of Natural Science and Technology, Okayama University
  • IMAMURA Koreyoshi
    Division of Chemistry and Biochemistry, Graduate School of Natural Science and Technology, Okayama University
  • NAKANISHI Kazuhiro
    Division of Chemistry and Biochemistry, Graduate School of Natural Science and Technology, Okayama University

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  • Purification, Characterization, Molecular Cloning, and Expression of a New Aminoacylase from Streptomyces mobaraensis That Can Hydrolyze N-(Middle/Long)-chain-fatty-acyl-L-amino Acids as Well as N-Short-chain-acyl-L-amino acids
  • Purification, characterization, molecular cloning, and expression of a new aminoacylase from Streptomyces mobaraensis that can hydrolyze N-(middle/long)-chain-fatty-acyl-l-amino acids as well as N-short-chain-fatty-acyl-l-amino acids

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We report here on the purification, characterization, molecular cloning, and expression of a new aminoacylase, initially isolated from the supernatant of Streptomyces mobaraensis (Sm-AA). Purified wild-type Sm-AA was found to be a monomeric protein with a molecular mass of 55 kDa. The cloned gene of Sm-AA contained an ORF of 1,383 bp, encoding a polypeptide of 460 amino acids. A BLAST search revealed that Sm-AA belongs to the peptidase M20 family, with identities to a hypothetical protein from Streptomyces pristinaespiralis, a putative peptidase from Streptomyces avermitilis, peptidase M20 from Frankia sp., succinyl-diaminopimelate desuccinylase from Hemophilus influenzae, and aminoacylase-1 from porcine kidney at 89, 88, 67, 29, and 25% respectively. The Sm-AA gene was subcloned into an expression vector, pSH19, and was expressed in Streptomyces lividans TK24. The amount of the recombinant Sm-AA expressed in the S. lividans cells was approximately 42-fold higher than that of Sm-AA found in the supernatant of S. mobaraensis. Sm-AA showed high hydrolytic activity towards various N-acetyl-L-amino acids and N-(middle/long)-chain-fatty-acyl-L-amino acids, with a preference for the acyl derivatives of L-Met, L-Ala, L-Cys, etc. with an optimum pH and temperature for reaction of about 7.5 and 50 °C (at pH 7.5).

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