@article{oai:miyazaki-u.repo.nii.ac.jp:00003226,
 author = {中村, 豊彦 and Nakamura, Toyohiko and 浦川, 智博 and 水光, 正仁 and Suiko, Masahito and 太田, 一良 and Ohta, Kazuyoshi and Urakawa, Tomohiro},
 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 = {In our previous study, inulinase P-II, one of the two inulinases P-I and P-II, which are known to be produced by 12 strains of Aspergillus niger was purified to an electrophoretically single peak and its characterization was done. In the present study, we attempted to purify inulinase P-I from Aspergillus niger by ion-exchange chromatography in DEAE-Cellulose column and gel filtration in Sephadex column. The catalytic properties of this electrophoretically homogeneous enzyme were compared with those of inulinase P-II described in the previous report. The molecular weight of P- I was estimated to be 72,000 and 70,000 by Sephadex G-200 gel chromatography and SDS-PAGE, respectively, suggesting that P-I is a monomer enzyme. The optimum pH was 4.0 for P-I and 5.0 for P-II and the optimum temperature was nearly 50t for both enzymes. Either of the two was stable within the range of pH 4.0-7.0 and the activity was not affected by heat treatment at 50°C. Further, both enzymes exhibited specific activities to inulin, sucrose and raffinose, but not to levan and melezitose. The values of Km for inulin and sucrose were 0.40 and 7.14 mM for P-I, and 1.87 and 12.50 mM for P- II. Next, the effects of metal ions and inhibitors on the activities of P-I and P-II were investigated. Mn^2+ ion activated the both enzymes and Ag^+ and Hg^2+ ions showed nearly complete inhibition of them. In addition, Fe^3+ and PCMB had strong inhibitory effects on the both enzymes and only P-I was slightly resistant to the inhibition of EDTA.},
 pages = {93--101},
 title = {Aspergillus nigerの生産する細胞外エキソ型イヌリナ-ゼ(P-I)の性質について},
 volume = {43},
 year = {1997},
 yomi = {ナカムラ, トヨヒコ and ウラカワ, トモヒロ and スイコウ, マサヒト and オオタ, カズヨシ}
}