Isolation and Characterization of a β-Primeverosidase-Like Enzyme from Penicillium multicolor

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<I>p</I>-Nitrophenyl and eugenyl β-primeveroside (6-<I>O</I>-β-<small>D</small>-xylopyranosyl-β-<small>D</small>-glucopyranoside) hydrolytic activity was found in culture filtrate from <I>Penicillium multicolor</I> IAM7153, and the enzyme was isolated. The enzyme was purified as a β-primeverosidase-like enzyme by precipitation with ammonium sulfate followed by successive chromatographies on Phenyl Sepharose, Mono Q, and β-galactosylamidine affinity columns. The molecular mass was estimated to be 50 kDa by SDS–PAGE and gel filtration. The purified enzyme was highly specific toward the substrate <I>p</I>-nitrophenyl β-primeveroside, which was cleaved in an endo-manner into primeverose and <I>p</I>-nitrophenol, but a series of β-primeveroside as aroma precursors were hydrolyzed only slightly as substrates for the enzyme. In analyses of its hydrolytic action and kinetics, the enzyme showed narrow substrate specificity with respect to the aglycon and glycon moieties of the diglycoside. We conclude that the present enzyme is a kind of β-diglycosidase rather than β-primeverosidase.

収録刊行物

  • Bioscience, biotechnology, and biochemistry  

    Bioscience, biotechnology, and biochemistry 70(3), 691-698, 2006-03-23 

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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各種コード

  • NII論文ID(NAID)
    10018533569
  • NII書誌ID(NCID)
    AA10824164
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    09168451
  • NDL 記事登録ID
    7871963
  • NDL 雑誌分類
    ZR7(科学技術--農林水産--農産) // ZR2(科学技術--生物学--生化学) // ZP1(科学技術--化学・化学工業)
  • NDL 請求記号
    Z53-G223
  • データ提供元
    CJP書誌  CJP引用  NDL  J-STAGE 
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