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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- 荒木, 紀美 田中, 奈穂美 萩原, 歩美 波多野, 智子 小林, 幹彦 アラキ, モトミ タナカ, ナオミ ハギワラ, アユミ ハタノ, トモコ コバヤシ, ミキヒコ Araki, Motomi Tanaka, Naomi Hagiwara, Ayumi Hatano, Tomoko Kobayashi, Mikihiko 多糖ゲル 加水分解酵素 α-アミラーゼ ガラクタナーゼ トレハラーゼ アルギン酸リアーゼ polysaccharide-gel hydrolase α-amylase galactanase trehalase alginate-lyase P(論文) 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. 2010-03-19 jpn departmental bulletin paper https://jissen.repo.nii.ac.jp/records/1030 AN10494731 実践女子大学生活科学部紀要 47 71 77 https://jissen.repo.nii.ac.jp/record/1030/files/KJ00006289360.pdf application/pdf 1.7 MB 2010-03-19