Showing papers on "Xylanase published in 1971"

Studies on Xylanase from Trichoderma viride

Abstract: The crude enzyme preparation obtained by isopropanol-precipitation of a water-extract of wheat bran culture of Trichoderma viride was first fractionated with ammonium sulfate precipitation, followed by DEAE-Sephadex A-25 column chromatography. Two active fractions, F-1 and F-4, were obtained. Fraction F-4 was futher purified by column chromatography with CM-Sephadex C-50 and was finally crystallized by the addition of ammoniun sulfate to 35% saturation. This purified xylanase A was homogeneous as judged by ultracentrifugation and discelectrophoresis. Maximum conditions for the activity of crystalline xylanase were pH 3.5 and 50°C. The enzyme was stable in a concentrated solution below 40°C and between pH 2 and 7, but at low enzyme concentration, i. e. 9.7μg per ml, it was easily inactivated under these same conditions.

Studies on Xylanase from Trichoderma viride: Part I. Isolation and Some Properties of Crystalline Xylanase

Abstract: The crude enzyme preparation obtained by isopropanol-precipitation of a water-extract of wheat bran culture of Trichoderma viride was first fractionated with ammonium sulfate precipitation, followed by DEAE-Sephadex A-25 column chromatography. Two active fractions, F-l and F-4, were obtained. Fraction F-4 was futher purified by column chromatography with CM-Sephadex C-50 and was finally crystallized by the addition of ammoniun sulfate to 35% saturation. This purified xylanase A was homogeneous as judged by ultracentrifugation and discelectrophoresis. Maximum conditions for the activity of crystalline xylanase were pH 3.5 and 50°C. The enzyme was stable in a concentrated solution below 40°C and between pH 2 and 7, but at low enzyme concentration, i.e. 9.7 μg per ml, it was easily inactivated under these same conditions.