Final substrate concentration [PNP] = Initial concentration x initial volume / final reaction volume.

The inverse of the PNP concentration is the inverse of the substrate concentration.

Calculated Gradient = Y2 -Y1 ÷ X2 - X1.

Multiply the change in optical density per second by 60 in order to get the change in optical density per minute.

The inverse of V0 is the inverse of the initial rate.

Vmax is the inverse of the y-intercept.

Km is the inverse of the x-intercept in reverse (negative).

The first experiment was the basic assay, which was used to evaluate the reactants and observe how the enzymes functioned under perfect circumstances.

As time is a factor that impacts absorbance levels, the graph illustrates that absorbance steadily grew with time, and the following absorbance vs. time graphs will be compared to this graph.

When it comes to [PNP], the rate of reaction rises up to a degree as the substrate concentration increases.

Any increase in the substrate will have no influence on the rate of reaction once all of the enzymes have joined, because the available enzymes will be saturated and operating at their maximal rate.

The experiment looked at and assessed four different quantities of substrate: 200 l, 150 l, 100 l, and 50 l.

When the experiment is finished and the graph is made, it is assumed that the 200l would have the steepest slope because it contains the greatest volume, and the 50l will have the steepest slope because it contains the least volume.

This was incorrect since the Michaelis-Menten Curve did not create a smooth curve because only two of the four points could be utilized because they were aligned.

This might be due to a human error, such as not correctly inserting the cuvette into the spectrometer or introducing a sample before the spectrometer has been calibrated, which results in erroneous data.

Michaelis-Menten kinetics, when the rule is followed and Km is increased but Vmax stays unchanged, show evidence of this inhibition.

The starting rate was plotted against [PNP] and the inhibitor using the Lineweaver-Burke Plot, and it was discovered that the Vmax intersected the Y axis at the same point of 2.55 OD min -1.

The inhibitor's Km was increased to 1.25, while the [PNP] was increased to 0.69.

The lab's final observation, based on the graph, would be how the rate of reaction climbs as the pH rises.

In a typical pH vs rate of reaction lab, the pH rises as the rate of reaction increases until it reaches an optimal pH, at which point the enzyme denatures and the pH falls.

In this experiment, the pH climbs until it reaches a maximum of 9.5, after which it falls slightly downward.

As there is no evidence that the pH has dropped below ideal levels, an error such as failing to keep the substrate on ice until ready to use or a change in the substrate concentration might have led to these false results.