<i>Bifidobacterium longum</i> JCM1217由来の組換えβ-Fructofuranosidaseの性質

DOI 日本農学文献記事索引 Web Site Web Site 参考文献33件
  • 大森 俊馬
    酪農学園大学大学院酪農学研究科食品栄養科学専攻
  • 上野 敬司
    酪農学園大学大学院酪農学研究科食品栄養科学専攻
  • 菊地 政則
    酪農学園大学大学院酪農学研究科食品栄養科学専攻
  • 小野寺 秀一
    酪農学園大学大学院酪農学研究科食品栄養科学専攻
  • 塩見 徳夫
    酪農学園大学大学院酪農学研究科食品栄養科学専攻

書誌事項

タイトル別名
  • Properties of Recombinant .BETA.-Fructofuranosidase from Bifidobacterium longum JCM1217
  • Properties of recombinant β-fructofuranosidase from Bifidobacterium longum JCM1217
  • Properties of recombinant v fructofuranosidase from Bifidobacterium longum JCM1217

この論文をさがす

抄録

We have investigated the enzymatic characterization of recombinant β-fructofuranosidase from Bifidobacterium longum JCM1217. This recombinant protein was expressed in Escherichia coli, and showed high activity of hydrolysis on fructo-oligosaccharides with a low degree of polymerization. The molecular mass of the purified recombinant protein was estimated to be about 64,000 by SDS-PAGE and 59,600 by MALDI TOF-MS. The optimum pH and pH stability of the enzyme were 5.7 and 5.0-7.9, respectively. The temperature stability of the enzyme was indicated up to 50°C. The Km (mM), Vmax (μmol/min/mg of protein), k0 (s-1) and k0/Km (mM-1 s-1) for 1-kestose, sucrose, neokestose, nystose, fructosylnystose and inulin were 1.2, 97, 96.4 and 80.3, 38, 64, 63.6 and 1.7, 2.1, 109, 105.3 and 50.1, 4.2, 52, 51.7 and 12.3, 3.1, 66, 65.6 and 21.2, 16.5, 72, 71.6 and 4.3, respectively. This recombinant protein had a high affinity for fructo-oligosaccharides.

収録刊行物

参考文献 (33)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ