PURIFICATION AND BIOCHEMICAL-CHARACTERIZATION OF AN ENDOXYLANASE FROMASPERGILLUS VERSICOLOR

An endoxylanase (beta-1,4-xylan xylanohydrolase, EC 3.2.1.8) was purif ied from the culture filtrate of a strain of Aspergillus versicolor gr own on oat wheat. The enzyme was purified to homogeneity by chromatogr aphy on DEAE-cellulose and Sephadex G-75. The purified enzyme was a mo nomer of molecular mass estimated to be 19 kDa by SDS-PAGE and gel fil tration. The enzyme was glycoprotein with 71% carbohydrate content and exhibited a pI of 5.4. The purified xylanase was specific for xylan h ydrolysis. The enzyme had a K-m of 6.5 mg ml(-1) and a V-max of 1440 U (mg protein)(-1). (C) 1998 Federation of European Microbiological Soc ieties. Published by Elsevier Science B.V. All rights reserved.