Preparation and enzymatic hydrolysis of maltosyl-.ALPHA.-cyclodextrin.

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  • SAKANO Yoshiyuki
    Laboratory Of Biological Chemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo Noko University
  • SANO Mutsumi
    Laboratory Of Biological Chemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo Noko University Present address: Central Research Laboratory, Takara Shuzo Co., Ltd.
  • KOBAYASHI Tsuneo
    Laboratory Of Biological Chemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo Noko University

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  • Preparation and Enzymatic Hydrolysis of Maltosyl-α-cyclodextrin

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Maltosyl-α-cyclodextrin (6-α-maltosylcyclomaltohexaose, M-CD) was prepared from maltose and α-cyclodextrin by the reverse action of Bacillus pullulanase, and the action of α-amylases on this dextrin was examined. Among α-amylases tested, Thermoactinomyces vulgaris α-amylase (TVA) and Taka-amylase A (TAA) were found to attack the M-CD. Their action pattern on M-CD was studied. These α-amylases cleaved, first the cyclodextrin ring of M-CD, and the branched octasaccharides formed were immediately degraded to form glucose, branched tetraose, or pentaose, though the action pattern was different for TVA and TAA. In addition, TAA also split M-CD into glucose and glucosyl-α-cyclodextrin. Fission products at various stages of the reaction were separated and analyzed by paper chromatography and high performance liquid chromatography, their structures were analyzed, and the degradation pattern of M-CD was found.

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