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The purified chitinase of Bacillus sp. R2 showed a molecular weight of 41.68 KDa, an optimal pH and temperature of 7.5 and 40°C respectively. The enzyme was stable between pH 7 to 8 but it lost 57% and 62% of its initial activity at the pH 6 and 9 respectively. The purified chitinase also exhibited complete heat stability for 1h at 40°C and retained above 50% and 30% of its original activity after...
The thermodynamic deactivation kinetics, ΔH * , ΔS * , E and ΔG * were used to understand the stability behaviour of the novel chitinases (I–III) of the marine isolate Pantoea dispersa in a range of salts and varying pH conditions (pH 4–9). The deactivation rate decreased with increasing half-life of chitinase I–III in the presence of salts at 30–60°C with the following effect...
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