Characterization of Endo-.BETA.-1,4-Glucanase and .BETA.-Glucosidase from Aspergillus sp. K-27.

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  • Abe Jun-ichi
    Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University
  • Nakanishi Taisuke
    Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University
  • Hizukuri Susumu
    Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University

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Other Title
  • Aspergillus　sp.　K-27のエンドβ-1,4-グルカナーゼとβ-グルコシダーゼの性質
  • Characterization of Endo-β-1,4-Glucanase and β-Glucosidase from Aspergillus sp. K-27
  • Characterization of Endo-ベーター1 4-Glucanase and ベーターGlucosidase from Aspergillus sp. K-27

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Abstract

Endo-β-1, 4-glucanase and β-glucosidase from Aspergillus sp. K-27 were purified to homogeneity. Endo-β-1, 4-glucanase was a monomeric enzyme with a Mr of .21, 000. Its activities for cellooligosaccharides were high in the order of cellohexaose>cellopentaose>cellotetraose, but no activity was recorded in cellobiose or cellotriose. It degraded carboxymethyl cellulose into cellobiose very well; however, almost no action was recorded on Avicel. β-Glucosidase was shown to be composed of two subunits of different molecular weights (Mr 130, 000 and 105, 000). The activities of the enzyme for different disaccharides were in the order of laminaribiose (β-1, 3) >gentiobiose (β-1, 6) >cellobiose (β-1, 4) > sophorose (β-1, 2). Using cellooligosaccharides as substrates, the enzyme was shown to have the largest and smallest Km/ Vmax values for cellotriose and cellobiose, respectively.

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