XYLANASE PRODUCED BY A PECULIAR, IMPERFEC T FUNGUS, FUSIDIUM SP BX-1

The degradation of xylan by an imperfect fungus, Fusidium sp. BX-1, wa s remarkably enhanced in a medium containing glycerol. Under these con ditions, the amount of xylan-degrading enzymes produced extracellularl y by strain BX-1 was about 15 times larger than that of the medium con taining only xylan as a carbon source. A xylanase from these enzymes w as purified and proved to be electrophoretically homogeneous. Its mole cular mass was estimated to be about 36,000. The optimum pH for its ac tivity was 5.5. The optimum temperature was 60-degrees-C. The enzyme w as stable within the range of 0-50-degrees-C and at pH 4.0-9.0. The en zyme could degrade xylotriose to xylose and xylobiose, but it was iner t to xylobiose and phenyl-beta-xyloside.