@article{oai:jissen.repo.nii.ac.jp:00001043,
 author = {荒木, 紀美 and 竹内, 梓 and 小林, 唯 and 柳田, 彩乃 and 河野, 祥子 and 関, 澄恵 and 池和田, 恵 and 小林, 幹彦 and アラキ, モトミ and タケウチ,アズサ /コバヤシ,ユイ /ヤナギダ,アヤノ and コウノ, サチコ and セキ, スミエ and イケワダ, メグミ and コバヤシ, ミキヒコ and Araki, Motomi and Takeuchi,  Azusa and Kobayashi, Yui and Yanagida, Ayano and Kouno, Sachiko and Seki, Sumie and Ikewada, Megumi and Kobayashi, Mikihiko},
 journal = {実践女子大学生活科学部紀要},
 month = {Mar},
 note = {P(論文), Trehalase activity in a homogenized preparation from the fruit body of king oyster mushroom (eryngii), Pleurotus eryngii was studied in detail. Distribution of trehalose and trehalase activity was higher in the cap (pileus) fraction than in the other positions such as stalk (stipe). The tretalase peak 1 was purified by the Sephacryl S-200 and Toyopearl HW-55 column chromatography. Electorophoretic analysis of trehalase gave values of molecular weight of 36~37kDa, and oligomeric forms and blycoprotein forms of trehalase were suggested by the band patterns of resulting gels. Optimum conditons of pH and temperature were determined to be pH5.0 and 30℃, respectively. Trehalase peak 1 showed higher reactivity to α-, α-trehalose, whereas peak 2 enzyme showed higher activity to β-,β-trehalose, methyl-β-glucoside, and cellobiose, indicating that this enzyme might have a substrate specificity such asβ-glucosidase.},
 pages = {19--25},
 title = {エリンギ(Pleurotus eryngii)のトレハラーゼ : 酵素の分布、精製および性質について},
 volume = {48},
 year = {2011}
}