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The enzyme shows reduced binding affinities for both substrates and inhibitors.
The purified enzyme shows unusual kinetics with a low affinity for both substrates.
Vmax was found as 0.02 μmol/min electrode for both substrates.
For both substrates, a dissociative adsorption Langmuir-Hinshelwood mechanism was found.
This sample has high UV activity and is comparable to Aeroxide P25 TiO2 reference photocatalyst for both substrates.
Very importantly, the calculations are able to reproduce and rationalise the enantioselectivity of the enzyme for both substrates.
Interestingly, a local QCR activity minimum is found for both substrates at 120 140 mM ionic strength.
A mathematical model that predicts the growth rate of the coating for both substrates is being proposed.
For both substrates, the productivity was considerably higher compared to data reported by other authors, demonstrating the robustness, efficiency, and stability of the selected biocatalyst.
There was good removal of organic matter for both substrates in terms of either protein (87 ± 6 97 ± 2%) or total COD (86 ± 2 91 ± 2%).
From the variation of rate with [S], the binding constants for both substrates involved in formation of the complex can be estimated.
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