Purification and Characterization of Endo-1,4-β-Xylanase from Pacilomyces varioti Bainier

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An endo-xylanase (1,4-β-D-xylanxylanohydrolase EC 3.2.1.8) was isolated from the culture filtrate of Paecilomyces varioti Bainier. The enzyme was purified 3.2 fold with a 60% yield by gel filtration and ionexchange chromatography. The purified enzyme had a molecular weight of 25,000 with a sedimentation coefficient of 2.2 S. The isoelectric point of the emzyme was 3.9. The enzyme was obtained in crystalline form. The optimum pH range was 5.5-7.0 and the temperature, 65℃. The Mechaelis constant was 2.5 mg larchwood xylan/ml. The enzyme was found to degrade xylan by an endo mechanism producing arabinose, xylobise, xylo-and arabinoxylxylo-oligosaccharides, during the initial stages of hydrolysis. On prolonged incubation, xylotriose, arabinosylxylotriose and xylobiose were the major products with traces of xylotetraose, xylose and arabinose.
公益社団法人日本生物工学会の論文
1989-02-25