褐藻ポリマンヌロン酸5-エピメラ-ゼの酵素的性質〔英文〕

概要

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The general enzymatic properties of algal polymannuronic acid 5-epimerase were investigated using Ishige okamurai, I. sinicola, and Hizikia fusiformis as starting materials. Its activity was optimal at pH 7.7 and at 30°C. The stability to pH was relatively high, while the enzyme was rather unstable to heat. The activity decreased gradually during storage at 4°C and even at -45°C. The enzyme showed its activity to a polymannuronate and to an alginate rich in mannuronic acid, but no activity to a polyguluronate. It was activated by Ca2+, Mn2+, and particularly by Mg2+, and strongly inhibited by Zn2+, Fe3+, and p-chloromercuribenzoate. The Km for polymannuronate was estimated to be 7.3×10-4 and the molecular weight to be 62, 000.
日本水産學會の論文