@article{oai:jissen.repo.nii.ac.jp:00001030,
 author = {荒木, 紀美 and 田中, 奈穂美 and 萩原, 歩美 and 波多野, 智子 and 小林, 幹彦 and アラキ, モトミ and タナカ, ナオミ and ハギワラ, アユミ and ハタノ, トモコ and コバヤシ, ミキヒコ and Araki, Motomi and Tanaka, Naomi and Hagiwara, Ayumi and Hatano, Tomoko and Kobayashi, Mikihiko},
 journal = {実践女子大学生活科学部紀要},
 month = {Mar},
 note = {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.},
 pages = {71--77},
 title = {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-},
 volume = {47},
 year = {2010}
}