Chemical Reaction Lab Report

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Recommended: Enzyme kinetics determining the effect of enzyme concentration activity

Discussion: In the experiment of enzyme kinetics, inhibition and concentration of substrate were investigated. The effect of these two factors will be determined through an experiment of four different concentrations of the inhibitor, and five different concentrations of substrate. Figures 2, 3, 4, and 5 provide an observation for the change in absorbance with time in the presence of different concentrations of inhibitor, and in the absence of inhibitor (phosphate). According to figure 6, the inhibitor is competitive as the Km value increases and Vmax value is constant. However, one LB plot that has [I] = 0.133 mM did not have the same characteristics of other inhibitors. So, this inhibitor may be mixed. True and apparent Km can be determined from table 9. The true Km is of [I] = 0 mM, so the other three Km are apparent Km. According to the results in table 9, Kmapp > Km. …show more content…

In fact, it indicates the concentration needed to produce half maximum inhibition. Ki =0.08 Conclusion: This experiment was very hard to do, and very long. However, it is a very important experiment as it determines the kind of inhibitor used and its effect on the chemical reaction. We think that we had good results. Objectives: The objective of this experiment is to determine enzyme catalytic activity, and to determine Km and Vmax values for an enzyme catalyzed reaction. Also, this experiment tend to investigate factors that influence rate of an enzyme catalyzed reaction. Abstract: In this experiment the purpose was to find Km and Vmax values. Also, the effect and type of inhibitors were the aim of enzyme kinetics experiment. Type of inhibition and true and apparent Km and Vmax were determined by LB plots, and the inhibitor constant Ki was determined by Dixon plot. The results indicated that the inhibitor is competitive and mixed, Kmapp > Km, Vmaxapp > Vmax, and

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