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In addition to exhibiting maximum reaction rates at lower temperatures, cold-adapted enzymes are more heat-labile and their catalytic mechanisms have distinct signatures in terms of the thermodynamic activation parameters.
Kinetic analysis revealed that only PhaJ4Pa exhibits almost constant maximum reaction rates (Vmax) irrespective of the chain length of the substrates.
The designed experiments indicate that maximum reaction rates reported in the literature were probably a consequence of the increasing CO2 concentration in the gas mixture when the inert gas was switched to CO2.
Maximum reaction rates (10.4 and 2.4 mmol/ld for aerobic respiration and denitrification respectively) and Michaelis constants (0.14 and 0.1 mmol/l for aerobic respiration and denitrification respectively) were determined.
For O2 reduction, for the oxidation of l-cysteine and of 2-mercaptoethanol when activity (as log k) is compared along the transition series volcano-shaped curves are obtained, which illustrates the concept of 'tuning' frontier orbital energies for maximum reaction rates.
To check this hypothesis, the corresponding maximum reaction rates are presented in Fig. 16.
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The maximum reaction rate and kinetic constants were matched with the order bi bi model.
For such conditions, the maximum reaction rate which can be determined from IS data is limited.
The flow velocity with the maximum reaction rate was 0.66 m/s, and it can be adjusted by changing windward area.
The maximum reaction rate varied between 3.5 μmol/min mg enzyme and 29.8 μmol/min mg enzyme.
The maximum reaction rate (Vmax) was 358.63 nmol min−1 and the Michaelis Menten constant (Km) was 37.33 mmol L−1.
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