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- W2364154360 abstract "In the present study, two kinds of D-xylanases (1, 4--D-xylan xylanohydrolase (EC 3.2.1.8) were purified and characterized from crude extract of Aspergillus niger KG79. Xylanase I was most active at pH 5.0, whereas xylanse II at pH 4.0 Both enzymes demonstrated their maximum activity at 45. They were relatively stable between pH 4.0 and 6.0 at 3 for 6 hours. Molecular weight of xylanse I and II were 12, 500 and 11, 500, respectively. Michaelis-Menten constants of xylanse I and II were 0.28% and 0.26% of xylan, respectively. Both enzymes could degrade commercial D-xylan to xylose, xylobiose, and xylotriose to the degree of about 10% of total reducing power. Xylanse I could, however, liberate arabinose from barley straw xylan in addition to xylose and xylooligasaccharides more rapidly than xylanase II. The degree of hydrolysis was about 25%. The reconstituted D-xylanase system with purified xylanases and -xylosidase degraded commercial xylan and barley straw xylan to the degree of 28% and 54% respectively. The limit of hydrolysis by the enzymes was suggested to be resulted from the physical structure of the substrate." @default.
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- W2364154360 date "1983-01-01" @default.
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- W2364154360 title "studies on hemicellulase system in aspergillus niger(1) -purification and reconstitution of D-xylanase-" @default.
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