Purification and biochemical characterization of an endoxylanase from Aspergillus versicolor |
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Authors: | Eleonora Cano Carmona,Marcia Regina Brochetto-braga,Aline Aparecida Pizzirani-kleiner,Joã o Atilio Jorge |
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Affiliation: | Centre d'Ingénierie des Protéines, Institut de Chimie, Universitéde Liège, B6, Sart Tilman, B4000 Liège, Belgium;Laboratoire de Biochimie, Institut de Chimie, Universitéde Liège, B6, Sart Tilman, B4000 Liège, Belgium |
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Abstract: | An endoxylanase (β-1,4-xylan xylanohydrolase, EC 3.2.1.8) was purified from the culture filtrate of a strain of Aspergillus versicolor grown on oat wheat. The enzyme was purified to homogeneity by chromatography on DEAE-cellulose and Sephadex G-75. The purified enzyme was a monomer of molecular mass estimated to be 19 kDa by SDS-PAGE and gel filtration. The enzyme was glycoprotein with 71% carbohydrate content and exhibited a pI of 5.4. The purified xylanase was specific for xylan hydrolysis. The enzyme had a K m of 6.5 mg ml−1 and a V max of 1440 U (mg protein)−1. |
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Keywords: | β-Lactamase Psychrophile Secretion Induction |
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