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Agricultural and Biological Chemistry
Vol. 49 (1985) No. 7 P 2033-2039



Xylanases from alkalophilic thermophilic Bacillus spp. W1 and W2 were purified and characterized. The xylanases from the two strains were fractionated into two active components (I and II) by DEAE-Toyopearl 650M chromatography. Components I from the two strains had similar properties: optimum pH, 6.0; optimum temperature, 65°C; isoelectric point, pH 8.5 and 8.3; molecular weight, 21, 500 and 22, 500; and Michaelis constant, 4.5 and 4.0mg-xylan/ml. Components II from the two strains also had similar properties: optimum pH, 7.0-9.0 and 7.0-9.5; optimum temperature, 70°C; isoelectric point, pH 3.6 and 3.7; molecular weight, 49, 500 and 50, 000; and Michaelis constant, 0.95 and 0.57mg-xylan/ml. The activities of components I and II were inhibited by Hg++ and Cu++. Components I hydrolyzed xylan to yield xylobiose and higher oligomers, but components II produced xylose other than xylobiose and xylooligomers.

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