追熟中のキウイフルーツ(Actinidia deliciosa(A.Chev.)C.F.Liang et A.R.Ferguson,cv.Haywaed)のα-グルコシダーゼの精製ならびに性状について

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  • Purification and Properties of α-glucosidase from kiwifruit (<I>Actinidia deliciosa</I> (A. Chev.) C. F. Liang et A. R. Ferguson, cv. Haywaed) during ripening
  • 追熟中のキウイフルーツ (<I>Actinidia deliciosa</I> (A. Chev.) C. F. Liang et A. R. Ferguson, cv. Haywaed) のα-グルコシダーゼの精製ならびに性状について
  • ツイジュクチュウ ノ キウイフルーツ Actinidia deliciosa A Chev C F Liang et A R Ferguson cv Haywaed ノ アルファ グルコシダーゼ ノ セイセイ ナラビニ セイジョウ ニ ツイテ

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α-Glucosidase of kiwifruit was purified by ammonium sulfate precipitation, followed by affinity chromatography (α-cyclodextrin sepharose 6 B), ion-exchange chromatography (DEAE-cellulose), gel filtration (Sephadex G-200) and isoelectric focusing (LKB8 100). The enzyme was found to be a single band when examined by electrophoresis. The specific activity of the enzyme purified was 294-fold of the crude extract enzyme. The α-Glucosidase had a molecular weight of 18, 000 and an isoelectric point of 4.9. And the highest activity was at pH 6. 5, 45t. α-Glucosidase was stable at pH 5.0-7.0 and below 40°C. The Km value for p-nitorophenyl-α-D-glucopyranoside of α-glucosidase was calculated to be 1.9mM. The enzyme activity was inhibited by 5, 5'-dithio-bis (2-nitrobenzoic acid), p-chloromercuribenzoic acid, Zn2+, Cu2+, Ni2+, Cd2+ and Hg2+. When qualitative thin-layer chromatographic analysis on the oligosacchraide hydrolysate solution digested by the enzyme, α-glucosidase produced a glucose from oligosaccharides. The enzyme specifically digested maltose, maltotriose, maltotrtraose, maltopentaose, and maltohexaose, but not amylose.

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