Mode of Action of a Minor Xylanase From Thermoascus aurantiacus on Polysaccharides and Model Substrates

摘要

The mode of action of a minor xylanase on a variety of polysaccharides and model substrates was investigated. The enzyme was excreted by Thermoascus aurantiacus grown in solid state fermentation (SSF). The purified enzyme had a molecular mass of 33,000. Thin layer chromatography analysis showed that the endoxylanase liberated short fragments from polysaccharides. The enzyme hydrolysed aryl-#beta#-d-cellobioside and the chromogenic (fluorogenic) 4-methylumbelliferyl-#beta#-glycosides of xylobiose (MeUmbXyl_2) and xylotriose (MeUmbXyl_3) at the agluconic linkage. The results suggested that the endoxylanase belonged to family 10.