Abstract
An endo-(1→3)-β- d-glucanase(EC 3.2.1.6), isolated from the culture filtrate of the fungus Mucor hiemalis, was purified by ammonium sulfate fractionation, gel filtration, and column chromatography on O-(carboxymethyl)cellulose. The optimum pH, optimum temperature, and K m value of the enzyme were pH 5.0, 50°, 0.048%, respectively. The enzyme was strongly inactivated by Pb 2+, Cu 2+, and Hg 2+ ions and also inhibited by Zn 2+ and Fe 3+ ions. The enzyme was specific for laminaran and the action pattern of the enzyme was of the endo-type. The molecular weight of the enzyme, as determined by gel filtration, was 30,000.
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