Reversion Product from D-Glucose by Crude Glucoamylase (<i>Endomyces</i> sp.)

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  • WATANABE Toshiyuki
    Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University
  • KAWAMURA Sugio
    Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University
  • TANNO Mutsuko
    Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University
  • MATSUDA Kazuo
    Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University

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Other Title
  • 糖化酵素剤 (<i>Endomyces</i> sp.) により生成する逆合成糖類について
  • トウカ コウソザイ Endomyces sp. ニ ヨリ セイセイ スル ギャクゴウセイ トウルイ ニ ツイテ

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Abstract

Product of reverse action of glucoamylase (Endomyces sp.) was prepared by incubating 40% D-glucose solution with 0.5% of crude glucoamylase (Matulase G) at 55°C for 72_??_96 hours, followed by inactivating the enzyme at 90°C for 10 minutes. By paper chromatography and paper ionophoresis, nigerose, maltose, isomaltose, laminaribiose, gentiobiose, panose, isopanose and isomaltotriose were detected in the reaction product. The amount of reversion product of Endomyces sp. was 6.5% of the total sugar. This value is twice as large as that of Rhizopus niveus (Gluczyme). Moreover, in the reversion product of Endomyces sp., the content of isomaltose fraction was larger than that of maltose fraction, while, in the reversion product of Rhizopus niveus, the latter was a little larger than the former.<br> Reversion product from 600g of D-glucose was fractionated by carbon-Celite column using water and 2.5_??_15% ethanol as successive elution solvents. Further separation of sugar was carried out by thick paper chromatography and also by Magnesol-Celite column chromatography of the acetylated sugars. In this way, nigerose, maltose, isomaltose, laminaribiose and gentiobiose were identified as their crystalline octaacetates. Panose was identified as crystalline panitol dodecaacetate. The crude enzyme (Matulase G) used in this experiment showed no transglucosylase activity.

Journal

  • Nippon Nōgeikagaku Kaishi

    Nippon Nōgeikagaku Kaishi 41 (9), 470-474, 1967

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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