3.1.2. Effect of pH on activity and stability of crude proteases
The activity of the crude enzyme was determined at differentpH values (5.0–12.0). As shown in Fig. 2a, two activity peakswere observed at pH 6.0 and 10.0. The enzyme preparation washighly active between pH 8.0 and 11.0, with an optimum at pH10.0. The relative activities at pH 9.0, 11.0, and 12.0 were about94%, 69%, and 39%, respectively, of that at pH 10.0. The opti-mum pH of S. scrofa proteases was similar to those of Colossomamacropomum proteases (Esposito et al., 2009a) and Lithognathusmormyrus proteases (El Hadj-Ali et al., 2011).
3.1.2. Effect of pH on activity and stability of crude proteasesThe activity of the crude enzyme was determined at differentpH values (5.0–12.0). As shown in Fig. 2a, two activity peakswere observed at pH 6.0 and 10.0. The enzyme preparation washighly active between pH 8.0 and 11.0, with an optimum at pH10.0. The relative activities at pH 9.0, 11.0, and 12.0 were about94%, 69%, and 39%, respectively, of that at pH 10.0. The opti-mum pH of S. scrofa proteases was similar to those of Colossomamacropomum proteases (Esposito et al., 2009a) and Lithognathusmormyrus proteases (El Hadj-Ali et al., 2011).
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