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The recombinant CgChoA was active between pH 4 8 with optimal activity in the neutral range similarly to other cholesterol oxidases (Table 1), e.g. at pH 6.75 using 0.011 M MOPS buffer for the coupled HRP assay.
The UppP phosphatase activity is metal dependent with a strong preference for the divalent cations magnesium and calcium, the latter giving optimal activity in vitro12, 13.
Then, several aspartate kinsases and dipicolinate synthases were screened for optimal activity in E. coli.
This enzyme has optimal activity in the temperature range of 70 90 °C and pH 10 11.
Catalytic test series for organic dye degradation and water oxidation show that template-free BiVO4 nanoplatelets obtained at pH 4 exhibit optimal activity in both processes.
These enzymes for the transformation of PPD-type ginsenosides including G-Rc showed optimal activity in the range pH 4.0 6.0 (Park et al. 2010; Yang et al. 2015).
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Using synthetic peptides together with MALDI-Tof-MS analyses, we demonstrated that the non-conserved 5-AA motifs flanking N-termini of the CLV3 and its orthologous CLE1 peptides were critical for their cleavages and optimal activities in vitro.
Results showed that encoding failure was associated with supra-optimal activity in the high-distraction condition and with sub-optimal activity in the low distraction condition.
The optimal activity distribution in catalyst pellets for reacting systems which undergo deactivation is analysed.
The optimal activity distribution in a catalyst pellet is studied experimentally for a reacting system undergoing poisoning.
These results suggest that the bacteria produce enzymes whose optimal activity occurs in different pH values.
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