purification and properties of an endoglucanase from thermoascus aurantiacus
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ID: 211831
2015
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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 35 kDa. Optimum temperature for the enzyme was found to be 70 °C and stability was upto 80 °C for 1 h. Along with higher stability at 80 °C, enzyme showed half lives of 192 h and 144 h 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 37 mg/ml and 82.6 U/min/mg protein respectively with higher salt tolerance of 10% for 1 h.
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dave2015biotechnologypurification
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| Authors | ;Bhaumik R. Dave;Ankit P. Sudhir;R.B. Subramanian |
| Journal | PLoS genetics |
| Year | 2015 |
| DOI |
10.1016/j.btre.2014.11.004
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