Purification and Properties of a Novel Thermoactive Endoglucanase from Aspergillus awamori VTCC-F099

A novel extracellular endoglucanase from Aspergillus awamori VTCC-F099 was purified 3.08-fold to homogeneity throughout gel filtration and ion exchange chromatography. Purified EG had a specific activity of 65.3 U/mg protein and a molecular mass of 32 kDa. Km and Vmax were 5.83 mg CMC/ml and 333.33 U/mg protein, respectively. Optimum temperature and pH were 50°C and 5, respectively. The enzyme was stable at up to 40°C and in pH range 4.5-5.5 with a residual activity of over 80% for 24 hours treatment. Fe2+, Cu2+ and EDTA activated EG activity whereas other metal ions, detergents and organic solvents inhibited the enzyme. These results suggested that EG from A. awamori VTCC-F099 could potentially be used as an additive in the feed for monogastric animals.