Application of the affinity binding of xylanases to oat-spelt xylan in the purification of endoxylanase CM-2 from Streptomyces chattanoogensis CECT 3336

The use of the insoluble polysaccharides Avicel and oat-spelt xylan for the binding and subsequent purification of active xylanases from Streptomyces chattanoogensis was investigated. Maximum recovery of xylanases was achieved with oat-spelt xylan, using NaCl (2 M) to remove active protein. The application of this technique to the purification of xylanases resulted in the purification of an endoxylanase (CM-2) with high specific activity (729.5 U mg(-1)). The properties of the purified enzyme, exhibiting activity and stability between 40 degrees C and 60 degrees C and between pH 5 and 8, suggest a potential role for both the enzyme and the rapid purification protocol in the removal of hemicelluloses from kraft pulp prior to bleaching.