@article{oai:miyazaki-u.repo.nii.ac.jp:00003229,
 author = {中村, 豊彦 and Nakamura, Toyohiko and 藤田, 平 and 太田, 一良 and Ohta, Kazuyoshi and Fujita, Taira},
 issue = {2},
 journal = {宮崎大学農学部研究報告, Bulletin of the Faculty of Agriculture, Miyazaki University},
 month = {Feb},
 note = {Our previous study demonstrated that the extracellular inulinase from a strain, Aspergillus niger 12 is a new endo-inulinase which is specific only to inulin but not to sucrose and raffinose etc. In this study, the endo-inulinase purified to electrophoretically homogeneous was immobilized onto amino-cellulofine according to carbodiimide coupling method. The activity yield of the immobilized enzyme was 35%.
The characteristics of the immobilized enzyme were compared with those of the native enzyme. The optimun pH was around 5.0 for the both enzyme and the optimum temperatures were 45°C for the native and 40°C for the immobilized enzyme. These results indicate that the immobilization resulted in the lowering of optimum temperature by 5°C. In addition, pH stability of the enzyme became broader and temperature stability was raised by approximately 10°C by the immobilization.
Then, the effects of various reagents on the enzyme activity were examined. An activation by Mn^2+, and strong inhibitions by Hg^2+, Ag^+ and NBS were found for both enzymes.},
 pages = {103--109},
 title = {Aspergillus nigerの生産する細胞外エンド型イヌリナ-ゼ(P-III)の固定化と性質},
 volume = {43},
 year = {1997},
 yomi = {ナカムラ, トヨヒコ and フジタ, タイラ and オオタ, カズヨシ}
}