Purification and Characterization of Isoamyl Alcohol Oxidase ("Mureka"-Forming Enzyme).

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  • YAMASHITA Nobuo
    Research and Development Department, Hakutsuru Sake Brewing Co. Ltd.
  • MOTOYOSHI Toru
    Research and Development Department, Hakutsuru Sake Brewing Co. Ltd.
  • NISHIMURA Akira
    Research and Development Department, Hakutsuru Sake Brewing Co. Ltd.

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  • Purification and Characterization of Isoamyl Alcohol Oxidase (“<i>Mureka</i>”-Forming Enzyme)

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Abstract

  Isoamyl alcohol oxidase (IAAOD) was purified to apparent homogeneity on SDS-PAGE from ultrafiltration (UF) concentrated sake. IAAOD was a glycoprotein, a monomeric protein with an apparent molecular mass of 73 and 87 kDa, by SDS-PAGE and gel filtration on HPLC, respectively.<br>   IAAOD showed high substrate specificity toward C5 branched-chain alkyl alcohol (isoamyl alcohol), and no activity toward shorter (C1-C4) or longer (C7-C10) alkyl alcohols tested. IAAOD was stable between pH 3.0-6.0 at 25°C. The optimum pH was 4.5 at 35°C. Heavy metal ions, p-chloromercuribenzoate (PCMB), hydrazine, and hydroxylamine strongly inhibited the enzyme activity, and an anti-oxidant like L-ascorbate did also.<br>   Isovaleraldehyde was produced markedly in pasteurized sake by adding purified IAAOD, therefore, we concluded that it was the enzyme that causes formation of mureka, an off-flavor of sake, the main component of which is isovaleraldehyde.<br>

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