Unidad de Bioingeniería, Instituto de Agroquímica y Tecnología de Alimentos, CSIC, Jaime Roig 11, 46010 Valencia, Spain; Unidad de Cereales, Instituto de Agroquímica y Tecnología de Alimentos, CSIC, Jaime Riog 11, 46010 Valencia, Spain
Abstract:
Abstract A neutral endoxylanase from a culture filtrate of Aspergillus nidulans grown on oat spelt xylan was purified to apparent homogeneity. The purified enzyme showed a single band on SDS-PAGE with a molecular mass of 22,000 and had an isoelectric point of 6.4. The enzyme was a non-debranching endoxylanase highly specific for xylans and completely free from cellulolytic activity. The xylanase showed an optimum activity at pH 5.5 and 62°C and had a K m of 4.2 mg oat spelt xylan per ml and a V max of 710 μmol min?1 (mg protein)?1.