DISCUSSION
Nelson et al, 2008, state “all enzymes that exhibit a hyperbolic dependence of V0 on [S] are said to follow Michaelis-Menten kinetics”. The data gathered from this experiment and plotted in figure 6 shows that it is this pattern shown in the reaction of PNPP to PNP catalysed by acid phosphatase, where a hyperbolic curve is observed in the graph of rate of reaction against substrate concentration, approaching the Vmax asymptotically. Acid phosphatase behaved congruently to the Michaelis-Menten model.
Vmax was determined as 6.65 x 10-3 µmol/min using the Lineweaver-Burk plot. However, as was highlighted in the results, one of the experimental data points produced a rate of reaction of 6.89 x 10-3 µmol/min – greater than that of the maximum expected. It can be seen in figure 7 that, while there is certainly a strong linear correlation …show more content…
Nelson et al (2008) suggest this may be due to a loss of structure in one part of the protein that then destabilises the rest of the structure, resulting in a rapid unfolding.
The data indicates that, in acid phosphatase, this occurs between 50oC and 75oC, where reaction rate drops from 14.06 x 10-3 µmol/min to 1.21 x 10-3 µmol/min respectively. However, without further data points between these values, it is not possible to determine the narrow range where this occurs. The experiment could be improved by increasing the number of temperature values tested for within this range, in order to better determine where the enzyme denatures.
The results for varying pH showed a relatively efficient rate of reaction across the range of pH 4.0 to ph 5.5, with the optimum observed efficiency occurring at a pH of 5.5 and reaction rate of 5.24 x 10-3 µmol/min. Figure 10 showed a general bell-shape curve when rate of reaction was plotted against pH, although this was not an exact bell curve as we may have
Nelson et al, 2008, state “all enzymes that exhibit a hyperbolic dependence of V0 on [S] are said to follow Michaelis-Menten kinetics”. The data gathered from this experiment and plotted in figure 6 shows that it is this pattern shown in the reaction of PNPP to PNP catalysed by acid phosphatase, where a hyperbolic curve is observed in the graph of rate of reaction against substrate concentration, approaching the Vmax asymptotically. Acid phosphatase behaved congruently to the Michaelis-Menten model.
Vmax was determined as 6.65 x 10-3 µmol/min using the Lineweaver-Burk plot. However, as was highlighted in the results, one of the experimental data points produced a rate of reaction of 6.89 x 10-3 µmol/min – greater than that of the maximum expected. It can be seen in figure 7 that, while there is certainly a strong linear correlation …show more content…
Nelson et al (2008) suggest this may be due to a loss of structure in one part of the protein that then destabilises the rest of the structure, resulting in a rapid unfolding.
The data indicates that, in acid phosphatase, this occurs between 50oC and 75oC, where reaction rate drops from 14.06 x 10-3 µmol/min to 1.21 x 10-3 µmol/min respectively. However, without further data points between these values, it is not possible to determine the narrow range where this occurs. The experiment could be improved by increasing the number of temperature values tested for within this range, in order to better determine where the enzyme denatures.
The results for varying pH showed a relatively efficient rate of reaction across the range of pH 4.0 to ph 5.5, with the optimum observed efficiency occurring at a pH of 5.5 and reaction rate of 5.24 x 10-3 µmol/min. Figure 10 showed a general bell-shape curve when rate of reaction was plotted against pH, although this was not an exact bell curve as we may have