The reaction rate of the uninhibited beta-galactosidase increased 6.83 times from 83 times the minimum (mean = 0.007 ± 0.000 mM/min) with an ONPG concentration of 3 mM to the maximum (mean = 0.046 ± 0.001 mM/min) with an ONPG concentration of 40 mM (Figure A1.1). With the presence of Inhibitor A, the beta-galactosidase enzyme activity increased 8.5 times from the minimum (mean = 0.004 ± 0.000 mM/min) with an ONPG concentration of 3 mM to the maximum (mean = 0.034 ± 0.001 mM/min) with an ONPG concentration of 40 mM (Figure A1.1). The trends for both the control (uninhibited) and the inhibited follow a logarithmic pattern. At 0 mM ONPG, both the control (uninhibited) and the inhibited beta-galactosidase reactions have the same reaction rate (mean = 0.000 ± 0.000 mM/min). At 40 mM, the reaction rate of the control (mean = 0.046 ± 0.001 mM/min) is 1.35 times faster than the inhibited hydrolysis of beta-galactosidase at the same concentration (0.034 ± 0.001 mM/min).