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However, the optimal activity is mainly obtained in the pH range of 3.0 5.0.
In the standard reaction condition (5 mM CaCl2) the enzyme was activated after incubation for 30 min and the optimal activity was retained for up to 2 h.
ScASNase1 was active in the range from pH 5.0 to 11.0, and its optimal activity was at pH 8.6 (Fig. 1C).
Optimal activity was achieved at 60 °C for H192P compared to 55 °C for wild type.
Optimal activity was observed upon removal of the pyrimidine C-4 chloro substituent.
The catalyst activity depended on the pyrolysis temperature, where the optimal activity was achieved by pyrolysis at 1073 1123 K.
Similar proteinase activity pH profiles were exhibited by root-fed and diet-fed rootworms with the optimal activity being slightly acidic.
On pNPX, optimal activity was achieved at pH 6 and 40 °C and Km and Kcat values were 2.92 mM and 1.32 seg−1, respectively.
Based on the application of a global desirability analysis on all the group of enzymes detected in the multienzyme solution, an overall optimal activity was observed at 53 °C and pH 4.7.
The result shows that the optimal activity was found for 7-μm-long TiO2 tubes, and tubes longer than 7 μm have thinner walls; thus, light is absorbed on a longer distance and pollutant has to diffuse further to reach the oxidizing species [30].
The optimal activity was at pH 6.4 and 70°C.
