Abstract
An Arthrographis sp. strain F4 xylanase was purified by acetone fractionation, ion-exchange on DEAE-Sephadex A-50 and Sephadex G-200 gel-filtration techniques. Its relative molecular mass (Mr) was estimated to be 28 100. The xylanase was optimally active at 55°C, pH 5.5, and stable at 40°C and pH 5.0–6.0. Significant inhibition (P 0.05). The Km value for oat splets xylan was 7.7 mg ml−1.
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