Purification and Properties of β-1,3-Glucanase from Lentinus lepideus

概要

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A β-1.3-glucanase from the culture medium of Lentinus lepideus was purified by DEAE-Sephadex A-25 column chromatography and Biogel P-100 gel filtration. The molecular weight of this enzyme was estimated to be 23,000 by the gel filtration method. The maxmum activity of this enzyme was obtained at about 45℃ and pH 5.0,the thermal and pH stable ragnes were up to 45℃ and from pH 5.0 to 6.0,respectively. The activity was inhibited by Hg^<++>, Ag^+, and p-chloromercuribenzoate. The K_m value for laminarin was determined to be 0.05%. This enzyme also acted feebly on pachyman and yeast glucan. This enzyme hydrolyzed laminarin in a random manner, finally yielding laminaribiose and glucose. This suggests that this enzyme is the smaller oligosaccharide-producting type of endo-β-1,3-glucanase.
公益社団法人日本生物工学会の論文
1978-10-25