When βF24G was used for ampicillin synthesis under kinetic control at industrially relevant conditions, 95% of nucleophile 6-aminopenicillanic acid (6-APA) was converted to ampicillin in aqueous medium at room temperature while 12% process time is needed to reach maximum product accumulation at 25% enzyme concentration compared with the wild-type Af PGA.
All the carbon sources tested exhibited maximum enzyme production at 10 mg/mL concentration.
The rate of the reaction should increase and reach the maximum value if the amount of enzyme concentration is kept constant and the substrate concentration is gradually increased.
The Vmax and Km were calculated by non-linear fitting (Prism5 from GraphPad) using the equation: where V is the observed enzyme velocity (activity), Vmax is the maximum enzyme velocity, S is the substrate concentration, and Km is the Michaelis-Menten constant.
Therefore, maximum velocity values (Vmax) related to total enzyme concentration are reported instead of kcat values.
Optimum enzyme concentration was determined by visualizing maximum fragment concentration in the 100- to 300-kb range.
The maximum enzyme conversion rate (Vmax) and the residual antibody concentration in the plasma and normal tissue were seen to be key determinants of drug concentration and drug-prodrug ratios in the tumour and other organs.
(2) (3) (4) (5) (6) where Vmax is the maximum enzyme velocity, Vapp the apparent maximal enzyme velocity, S the concentration of the substrate being varied, I the inhibitor concentration, K m the apparent Michelis Menten constant for S, S0.5 the half-saturation concentration for S, n the apparent Hill coefficient for S, Kis and Kii the dissociation constants of the [I] for E and ES, respectively.
A maximum saccharification rate of 88% was obtained at an enzyme concentration of 37.5 FPU/g-substrate after optimization of the hydrolysis parameters.
Maximum yields for shea oils were obtained at the highest enzyme concentration.
