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Tiara Matusin Bo5

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Tiara Matusin BO5

Reaction rate (mM/ Minute) of β- galactosidase increased as the concentration of ONPG (mM) went from 0 to 40 mM., this trend was noticeable with and without inhibitor A (Figure 1). The uninhibited enzyme reacts faster than the enzyme with inhibitor A. The Uninhibited enzyme that reacted with approximately 40mM of ONPG had the greatest reaction rate (0.046 ± 0.001), while the enzyme with inhibitor A reacted with 3mM of ONPG had the lowest reaction rate (0.004 ± 0.000). As the concentration of ONPG increases beyond 40mM the reaction rate of the uninhibited enzyme approaches a Vmax , of approximately 0.047. The Vmax of the enzyme with inhibitor A is about 0.035 as the concentration of ONPG goes beyond 40mM. When the concentration of ONPG was 11.5mM, the uninhibited enzyme reached its maximum catalytic efficiency (km). The enzyme with inhibitor A reached its km at approximately 16mM.


The Set of Values determined from the Line weaver- Burk plot are more accurate than the values determined from the Michaelis-menton plot because in the Michaelis-menton plot the Vmax is an asymptote, meaning that the value for Vmax is going to be an approximation and guess. With the data collected we were able to form a reciprocal graph (Line weaver- Burk plot) in which the slope of the line is Km/Vmsx, making the Vmax, the reciprocal of the y-intercept and the x-intercept equal to -1/km.  Finding the Vmax and Km is much easier, and more precise using the Line weaver- burk plot.  

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