Purification and properties of an endoglucanase of Aspergillus terreus DSM 826

✍ Scribed by Ali M. Elshafei; Mohamed M. Hassan; Bakry M. Haroun; Osama M. Abdel-Fatah; Housam M. Atta; Abdelmageed M. Othman

• Publisher: John Wiley and Sons
• Year: 2009
• Tongue: English
• Weight: 197 KB
• Volume: 49
• Category: Article
• ISSN: 0233-111X
• DOI: 10.1002/jobm.200800227

✦ Synopsis

Abstract

Endoglucanase (EG) from A. terreus DSM 826 grown on sugar cane bagasse as a carbon source was purified using acetone fractionation, then a Sepharose‐4B chromatographic column, with purification of about 27‐fold and 10.5% recovery. The optimum temperature and pH for activity of the purified EG were found to be 50 °C and pH 4.8, respectively. The purified enzyme can stand heating up to 50 °C for 1 h without apparent loss of activity. However, the enzyme, incubated at 80 °C for 5 min, showed about 56% loss of activity. Optimum EG activity was recorded with a citrate buffer system (pH 4.8; 0.05 M). Co^2+^ (2.5 × 10^–2^ M) and Zn^2+^ (5 × 10^–2^ M) were found to activate the purified EG of A. terreus DSM 826 by about 83 and 25%, respectively. On the other hand, Hg^2+^ inhibited the activity of the purified EG by about 50 and 71% at a concentration of 2.5 × 10^–2^ and 5 × 10^–2^ M, respectively. Carboxymethyl cellulose was found to be the best substrate for the purified EG, with V~max~ values of 4.35 μmol min^–1^ mg^–1^ protein. (© 2009 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)