フコイダンおよびフコイダン様多糖 V  アワビ肝臓中のフコイダン分解酵素 1  粗酵素とCM‐セルロース非吸着画分

書誌事項

タイトル別名
  • Enzymes in Hepatopancreas of Abalone Active on Fucoidan
  • アワビ カン スイゾウチュウ ノ フコイダン ブンカイ コウソ ニ ツイテ 1
  • (1)粗酵素とCM一セルロース非吸着画分

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Enzymes contained in hepatopancreas of abalone were investigated from a viewpoint of structural study of fucoidan. Results obtained were as follows.<br> 1. Fucoidan sulfatase activity together with fucoidanase activity were observed in a fraction (crude enzyme) precipitated from 30 to 50% saturation of ammonium sulfate.<br> 2. Each activity was separated into two fractions, unadsorbed and adsorbed fraction on CM-Cellulose at pH 5.0. Both activities of the unadsorbed fraction were eluted in the same elution range (Enzyme I) from DEAE-Cellulose column by gradient elution. Separation of both activities and inhibition either of them by using acid, alkali, or heat were unsuccessful.<br> 3. Rate of reducing sugar formation was decreased with reaction period in case of the crude enzyme, while it remained constant during reaction in case of Enzyme I. Decreased rate of sulfate ion formation was observed in both cases.<br> 4. Sugars formed by the crude enzyme were almost fucose. However, sugars formed by Enzyme I were primarily neutral oligosaccharides, and their polymerization degree showed a tendency to diminish with reaction period.<br> From the above evidence, it is considered that fucoidanase which degrades fucoidan to oligosaccharide, but not to fucose, and fucoidan sulfatase are existent in Enzyme I, and that, therefore, a method of investigation for partial degradation of fucoidan will be available by these enzymes.

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