Abstract
An Endo-cellulase was purified to homogeneity using ammonium sulfate precipitation, ion exchange and size exclusion chromatography from newly isolated strain of Thermoascus aurantiacus RBB-1. The recovery and purification fold were 13.3% and 6.6, respectively, after size exclusion chromatography. The purified cellulase has a molecular mass (M) of 35kDa. Optimum temperature for the enzyme was found to be 70°C and stability was upto 80°C for 1h. Along with higher stability at 80°C, enzyme showed half lives of 192h and 144h at 50 and 70°C respectively. The purified cellulase was optimally active at pH 4.0 and was stable over a broad pH range of 3.0–7.0. The enzyme purified showed apparent Km and Vmax values of 37mg/ml and 82.6U/min/mg protein respectively with higher salt tolerance of 10% for 1h.
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