糸状菌の大・裸麦β- グルカン分解酵素

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The properties of the enzyme extracts of 3 fungi capable of hydrolysing barley β-glucan; takadiastase (commercial diastase), Trichoderma koningi (commercial cellulase), and Mucor sp., were examined. The results showed that fungal β-glucanases owe most of their activities to β-1,3 glucanase, β-1,4 glucanase or β-glucosidase and hydrolyse β-glucan to the extent of 100 per cent as glucose, indicating that there are β-glucan hydrolysing activities which may not be attributed to the combined action of these enzymes.On the other hand, we have successively obtained the highly purified β-glucanase preparation from the extract of bran culture of Mucor sp., employing fractionation using ammonium sulfate, rivanol treatment, acetone precipitation, passing it through Duolite A_2 resin column, and then chromatography on Duolite CS-101 resin column, and finally with starch-zone electrophoresis. The preparation was homogeneous in free-boundary electrophoretic and ultracentrifugal analyses, and free from β-1,4 glucanase and β-glucosidase activity, but showed a weak activity of β-1,3 glucanase. The specific activity of the purified preparation rose 76-fold over the original extract, and 12 per cent of the starting activity was recovered.At optimum condition (pH 5.5,40℃) β-glucan and laminarin were hydrolyzed and liberated the glucose to the extent of 55% and 29% respectivety. The purified preparation acts on β-glucan in a random fashion producing 3-0-β-cellobiosyl D-glucose(23 per cent), 3-0-β-cellotriosyl D-glucose (10.5 per cent), laminaribiose, glucose, and higher oligosaccharides. Judging from the basic structure of barley β-glucan (Parrish et al. (1960)), it is clear that β-glucanase action had hydrolysed β-1,4 glucosidic linkage, and not β-1,3 linkage. These results are in agreement with opinions of Parrish et al.(1960) and Cunningham et al. (1964) concerning the specificity of laminarinase, but it might be difficult to explain that β-glucanase corresponds to laminarinase, since the specificity of β-glucanase upon laminarin is very low.Mucor sp. β-1,3 glucanases were also found to be fractionated into two components by zone electrophoresis : one is coincident with the β-glucanase peak and the other component with greater mobility than that of the β-glucanase peak.
社団法人日本生物工学会の論文
1965-09-25

糸状菌の大・裸麦β- グルカン分解酵素

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