Enzymes in Hepatopancreas of Abalone Active on a Sulfated Polysaccharide from Brown Seaweed <i>Undaria pinnatifida</i> (Harvey) Suringar, Wakame

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  • FUJIKAWA Tatsuo
    Department of Food Science and Technology, Faculty of Agriculture, Kyushu University
  • ANNO Takahiko
    Department of Food Science and Technology, Faculty of Agriculture, Kyushu University Food Research Institute, Nippon Shinyaku Co., Ltd.
  • WADA Masafuto
    Department of Food Science and Technology, Faculty of Agriculture, Kyushu University

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Other Title
  • フコイダンおよびフコイダン様多糖の研究　ＩＶ　　ワカメの硫酸多糖に作用するアワビ肝すい臓中の酵素
  • ワカメ ノ リュウサン タトウ ニ サヨウスル アワビ カン スイゾウチュウ

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Abstract

In connection with the structural study of galactofucan sulfate (sulfated polysaccharide of Undaria pinnatifida, Wakame), galactofucanase and α-L-fucosidase existing in hepatopancreas of abalone (Haliotis sp.) were investigated.<br> In a crude mixture of enzymes prepared from hepatopancreas, galactofucan sulfatase, arylsulfatase, and β-D-galactosidase were detected bisides galactofucanase and α-L-fucosidase. From the crude mixture, two partially purified fractions (FS-1 and FS-2) were obtained by column chromatography on DEAE-cellulose followed by gel filtration on Sephadex G-200. FS-1 showed the α-L-fucosidase activity and was free from the activity of galactofucanase and galactofucan sulfatase. FS-2 showed four activities of galactofucanase, galactofucan sulfatase, arylsulfatase, and fucoidanase and was free from the α-L-fucosidase activity. These results indicate that the galactofucanase may be endo-type enzyme and the same one as the fucoidanase. FS-1, however, showed an activity on the partially degraded galactofucan sulfate, and contained two types (optimum pH 3 and 5) of α-L-fucosidase: one with optimum pH 3 was inhibited with galactofucan sulfate and the other with optimum pH 5 was not inhibited.<br> From these results, it is considered that α-L-fucosidase in FS-1 are useful for the structural study of a fucoidan analogue due to their specificity on the substrate, and that the galactofucanase in FS-2 is useful for partial degradation of the fucoidan analogue.

Journal

  • Nippon Nōgeikagaku Kaishi

    Nippon Nōgeikagaku Kaishi 50 (12), 577-584, 1976

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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