Xylan-Containing supports used to separate xylanase from the cellulases of aspergillus terreus F-413

The separation of xylanase from cellulolytic enzymes of A. terreus F-413 by affinity chromatography on xylan-containing supports was investigated. Xylanase purified over tenfold was obtained after column chromatography on xylan bound to controlled porous glass. The molecular weight of the purified enzyme has been found to be 140 000 daltons, and it is homogeneous in polyacrylamide gel electrophoresis. Purified xylanase also showed residual celluloytic activity (perhaps cross-specificity) with cellulosic substrates.