Konjac-mannanase from the Tubers of Amorphophallus konjac C. Koch
1973 年 37 巻 1 号 p. 9-17
詳細
1973 年 37 巻 1 号 p. 9-17
A crude enzyme preparation hydrolyzing konjac mannan was extracted from germinating konjac tubers, and purified by chromatography with DEAE-cellulose and alkali-swollen cellulose, and by gel-filtration on Sephadex G-100. The purified enzyme preparation showed optimal activity at pH 4.7, optimum temperature at 40°C. It was considerably stable at pH's between 4.0 and 8.0, but inactivated rapidly by temperaters above 50°C. Hydrolysis of the mannan by this enzyme proceeded by typical random mechanism, and the rate was in agreement with an empirical equation, p=0.43 E0.77 t0.5. As the Km and Vmax Values for mannan, 7.14×10-2 (%) and 23.8×10-3 (_??_OD500nm) were obtained, respectively.
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