Purification and characterization of a novel thermostable α-l-arabinofuranosidase (α-l-AFase) from Chaetomium sp.

► A novel α-l-arabinofuranosidase was purified from Chaetomium species. ► The optimal pH and temperature of the enzyme were pH 5.0 and 70 °C, respectively. ► The enzyme showed high substrate specificity for the a-l-arabinofuranosyl linkage. ► The full-length cDNA of α-l-AFase gene (CsAra) of 1745-bp was obtained.