16) 酵母細胞壁溶解酵素にかんする研究 (第2報) : 溶解酵素系の分画

概要

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Enzyme(s) active in hydrolyzing yeast cell wall could be produced adaptively by a strain of Streptomyces albidoflavus. Yeast glucan was shown to be an effective inducer. Fractionation of the enzyme system was effected by using DEAR-cellulose column. In the effluent diagram, two peaks appared with regard to lytic activity ; one corresponded to the peak of protelytic activity and the other to that of β-1,3-glucanase activity. Thus, two fractions (prosease and β-1,3-glucanase fractions) could be isolated. The latter fraction was purified further by means of zone-electrophoresis until it showed a single peak where protein and glucanase activity curves overlapped. The purified fraction degraded yeast glucan and laminarin yielding biose and triose.The above two fractions, when used in conjunction, hydrolyzed yeast cell wall synergistically indicating that some polypeptide is impreganated as a binding material in the structure of yeast cell wall.Protease of quite different origin, such as Bacillus subtilis protease or papain, could not be the substitute for the protease fraction in the above action. Only "pronase", a proteolytic enzyme from Str. griceus, had a weak lytic activity and played partly the role similar to our protease fraction in the above-mentioned synergism.
社団法人日本生物工学会の論文
1963-07-15