多糖ゲルによる糖質加水分解酵素のアフィニティ-クロマトグラフィ-

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  • タトウ ゲル ニ ヨル トウシツ カスイ ブンカイ コウソ ノ アフィニティー クロマトグラフィー

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Soluble starch, pectic acid and alginic acid were cross-linked by polyacrylamide. Several enzymes, including commercially available specimen and food material sources, were examined for their specificities to the polysaccharide gels. α-Amylase showed high affinity for the starch-gel in the presence of 3M ammonium sulfate and eluted with the buffer solution containing no ammonium sulfate. Pectinase and alginate-lyase bound to the pectin-gel and the alginate-gel, respectively. On the other hand, galactanase form the common bean (Phaseolus vulgaris L) bound to the starch-gel ; however, trehalase did not bound to this gel. Highly purified alginate-lyase was obtained by the current affinity chromatography method. Based on these results, relationship between the chemical structure of the polysaccharide-gels and the substrate specificity of the enzymes was discussed.

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