Two xylanases were purified from the crude filtrate after growth of
T. inhamatum in liquid cultures with xylan, under optimized culture
conditions. Xyl II was purified to electrophoretic homogeneity by a
single step of ion exchange chromatography, while Xyl I purification
required a subsequent molecular exclusion chromatography with
Sephadex G-75. The first step (Fig. 1) revealed two protein peaks with
xylanolytic activity: Xyl I, corresponding to the not retained fraction,
presented 62.7% of the activity, and Xyl II, the retained fraction was
eluted with a NaCl gradient and presented 3.7% of the activity.