Characterization of a New (<i>R</i>)-Hydroxynitrile Lyase from the Japanese Apricot<i>Prunus mume</i>and cDNA Cloning and Secretory Expression of One of the Isozymes in<i>Pichia pastoris</i>

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  • FUKUTA Yasuhisa
    Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University
  • NANDA Samik
    Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University
  • KATO Yasuo
    Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University
  • YURIMOTO Hiroya
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
  • SAKAI Yasuyoshi
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
  • KOMEDA Hidenobu
    Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University
  • ASANO Yasuhisa
    Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University

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タイトル別名
  • Characterization of a New (R)-Hydroxynitrile Lyase from the Japanese Apricot Prunus mume and cDNA Cloning and Secretory Expression of One of the Isozymes in Pichia pastoris
  • Characterization of a new (R)-hydroxynitrile lyase from the Japanese apricot Prunus mume and cDNA cloning and secretory expression of one of the isozymes in Pichia pastoris, Biosci

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PmHNL, a hydroxynitrile lyase from Japanese apricot ume (Prunus mume) seed was purified to homogeneity by ammonium sulfate fractionation and chromatographic steps. The purified enzyme was a monomer with molecular mass of 58 kDa. It was a flavoprotein similar to other hydroxynitrile lyases of the Rosaceae family. It was active over a broad temperature, and pH range. The N-terminal amino acid sequence (20 amino acids) was identical with that of the enzyme from almond (Prunus dulcis). Based on the N-terminal sequence of the purified enzyme and the conserved amino acid sequences of the enzymes from Pr. dulcis, inverse PCR method was used for cloning of a putative PmHNL (PmHNL2) gene from a Pr. mume seedling. Then the cDNA for the enzyme was cloned. The deduced amino acid sequence was found to be highly similar (95%) to that of an enzyme from Pr. serotina, isozyme 2. The recombinant Pichia pastoris transformed with the PmHNL2 gene secreted an active enzyme in glycosylated form.

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