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The maximum enzyme activity was 855 ± 13 U/g.
The predicted value was verified experimentally, and the maximum enzyme activity reached 492 U/ml.
In optimization experiments, the maximum enzyme activity was found at pH 4.8 when incubated at 28°C for 11 days.
According to the RMS contour plots and variance analysis, the maximum enzyme activity was at 29.1 °C and pH 8.6.
The optimum pH and temperature for maximum enzyme activity of immobilized lipase are found to be pH 9 and 40 °C respectively.
RhaL1 anchored to the yeast cell surface showed maximum enzyme activity at pH 6.0 6.5 and 70 °C and was stable at pH 2.5 12.0 below 60 °C.
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Maximum enzyme activities occurred during the active phase of decomposition.
Repeated reuse of the adsorbed cells achieved the maximum enzyme specific activity after three cycles (33.86 U/mg protein).
Crushed maize was chosen as the solid substrate, for maximum polygalacturonase enzyme activity based on D-optimal design.
Considering the morphology of the final culture, Aspergillus sojae with the desired pellet morphology in a complex media, inoculated with a seed culture prepared from molasses resulted in maximum polygalacturonase enzyme activity (0.2 U/ml) and lowest suspension viscosity with a broth rheology close to Newtonian flow behavior.
Before reaching a maximum, the enzyme activity increased at a rate proportional to the increase in cell growth.
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