Lab Report Catalase

Results
Experiment I: As a general trend O2 production and reaction velocity increased with increasing catalase concentration, however, the 33% percent catalase concentration showed a drop of 0.175 mL O2/s compared to the 25% catalase concentration (figure 1.2). The velocity of 25% catalase was 0.275 mL/s, 33% was 0.1 mL/s, 50% was 0.435 mL/s, and 75% catalase was 0.575 mL/s (figure 1.1). The 50% catalase concentration produced the most O2 overall however the 75% catalase concentration had the fastest initial reaction velocity.
Experiment III: O2 production and reaction velocity increased until 30oC, after which both the velocity and O2 production decreased (figure 2.2). The reaction temperature with the fastest initial velocity was 30oC at
The 22.5% (6.615M), 27% (7.938M), and 30% (8.8M) H2O2 concentrations produced more than 50 mL of O2 and could not be measured past 75 seconds (figure 3.1). There is a drop in initial reaction velocity of 0.065 mL/s between 27% and 30% substrate concentration (figure 3.2). The substrate concentrations from slowest to fastest initial velocities are 3%, 7.5%, 15%, 22.5%, 30%, and 27%. The Vmax of the uninhibited reactions was 2.41 mL/s and the Km was 7.033M (figures 3.3 and 3.4). Generally, reaction rate increased with substrate concentration.
Experiment V: The substrate concentration with the fastest initial reaction velocity was 30% (8.8M) at 0.905 mL/s and the substrate concentration with the slowest initial reaction velocity was 3% (0.882M) at 0.145 mL/s (Figure 3.2). The substrate concentrations from slowest to fastest initial velocities are 3%, 7.5%, 15%, 22.5%, 27%, and 30%. The Vmax of the inhibited reactions was 1.208 mL/s and the Km was 7.033M (figures 3.3 and 3.4). Generally, reaction rate increased with substrate concentration.
A paired t-test was performed comparing the velocities for the inhibited (exp. V) and uninhibited (exp. IV) reactions. This t-test presented a p-value of
Both experiments showed an increase in velocity as H2O2 concentration increased from 3% (0.882M) to 27% (7.938M). While the velocity of experiment V (the inhibited reaction) continued to increase from 27% (7.938M) to 30% (8.8M) H2O2, the velocity of experiment IV (the uninhibited reaction) decreased slightly from 27% (7.938M) to 30% (8.8M) H2O2 (Figure 3.3). Since this is not an expected result based on Michaelis-Menten enzyme kinetics, this slight decrease was likely due to human error. The average difference in velocity between the inhibited and uninhibited reactions was 0.3942 mL/s. A paired t-test was run on the velocity data for the two experiments and resulted in a p-value of 0.001956. This result means that the differences in velocity between the inhibited and uninhibited results are statistically significant at a 99.8% confidence level. This means that there is a 0.1956% chance that the differences in velocity between the inhibited and uninhibited reactions are due to random chance. Based on these results it can be concluded that the sodium cyanide inhibitor reduces the reaction rate of enzyme-catalyzed reactions. The Vmax for the inhibited reaction was 1.208 mL/s and the uninhibited reaction was 2.41 mL/s. The Km for the inhibited reaction was 6.8611M and the Km for the uninhibited reaction was 7.2057M. These Km values were within 0.3446M of each