Cel5A (endoglucanase 11) of Trichoderma reesei was expressed in Saccharomyces cerevisiae then purified. Two components (Cl and C2) of recombinant Cel5A with different glycosylation were obtained. Purified Cl had a larger molecular mass (57 kDa) than that of the native Cel5A produced by T. reesei (48 kDa) due to the different extents of asparagines-linked glycosylation. There was no significant difference in enzymatic activity between the Cl and the native Cel5A from T reesei. Cl treated with Endoglycosidase H had a molecular mass of 54 kDa and retained about 88% of its original activity. Unpurified C2 was larger form of hyperglycosylation proteins. Its molecular mass was larger than 85 kDa till up to 200 kDa. It still retained activity regardless of its magnitude molecular mass. With increased glycosylation extent of the enzyme components (C2 > Cl > native Cel5A), the pH range of activity become wider, and thermal stability become higher. (c) 2007 Elsevier Inc. All rights reserved.