Chaetomium gracile変異株1161のキシラナーゼ : 精製およびキシロビオース生成に関する性質

概要

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A xylanase (CG) from a solid-state wheat-bran culture of Chaetomium gracile Mutant 1161 was purified by ethanol fractionation and CM-Sepharose CL-6B column chromatography. The purified CG was found to be homogenous on PAGE. The molecular weight was estimated to be 11,000 by Sephadex G-75 gel filtration, 19,000 by SDS-PAGE. 8M Urea-SDS-PAGE showed that this enzyme consisted of two subunits of 14,400 and 4,800. The isoelectric point was 8.35. The enzyme was inactivated by NBS, SDS, PCMB, and HgCl_2. The maximum xylobiose (X_2)-forming activity (ability) was shown at pH 5.0 and 50℃; pH and thermal stability ranges were at pHs 4.0〜7.0 and up to 45℃. The purified CG could not hydrolyze X_2. From an analysis of the bond cleavage of xylooligosaccharide-alditols, it was found that the first bond from the non-reducing end of oligosaccharides was not attacked, but the other bonds were hydrolyzed by endo-type action. At the maximum hydrolysis (more than 90%) of birch wood xylan, this xylanase produced X_2 to 74〜78% of the hydrolysates.
社団法人日本生物工学会の論文
1992-03-25