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
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- TANIGUCHI (YAMADA) Akiko
- Department of Brewing and Fermentation, Junior College of Tokyo University of Agriculture
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- TANIGUCHI Masayuki
- Department of Applied Biology and Chemistry, Faculty of Applied Bioscience, Tokyo University of Agriculture
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- TAKANO Katsumi
- Department of Applied Biology and Chemistry, Faculty of Applied Bioscience, Tokyo University of Agriculture
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- MATSUMOTO Shinji
- Food Processing Center, Faculty of Applied Bioscience, Tokyo University of Agriculture
Bibliographic Information
- Other Title
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- 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
- 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
- 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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Description
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.
Journal
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- Food Preservation Science
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Food Preservation Science 27 (3), 133-139, 2001
Japan Association of Food Preservation Scientists
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Details 詳細情報について
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- CRID
- 1390282680095621760
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- NII Article ID
- 10012770916
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- NII Book ID
- AA11178236
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- ISSN
- 21861277
- 13441213
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- NDL BIB ID
- 5818214
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- Data Source
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- JaLC
- IRDB
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed