Virtual Investigation of an Enzyme. A new protease (ref. no PR/66-430-010), isolated from B.yorkii has been characterised. A series of experiments were run on the enzyme to determine the optimum pH for the enzyme to run at, the effect of pH on KM and Vmax

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Biol 201 Workshop – A Virtual Investigation Of An Enzyme

Summary

  1. A new protease (ref. no PR/66-430-010), isolated from B.yorkii has been characterised.
  2. A series of experiments were run on the enzyme to determine the optimum pH for the enzyme to run at, the effect of pH on KM and Vmax, to determine the effect of azide on substrate binding, on the catalytic process itself or both and also to determine the dissociation constant for the enzyme-azide complex and the accuracy of the measurements.
  3. Experiments performed on the isolated enzyme showed that if the pH of the solution was too high then the rate of reaction is too slow to gain any results and the same was true if the ph is too low.
  4. The optimum pH was found to be pH 7.0
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Results

Fig.1 shows that the optimum pH at which the enzyme works at was pH 7.0.

Fig.2 is a Lineweaver-Burk plot of the reciprocal values of the enzyme recorded at ph 7.0, with all values constant other than the concentration of the substrate.

The Vmax and Km of the enzyme under inhibitor influence, double inhibitor and a control of no inhibitor were calculated from the lines of best fit on the plot and are as follows.

Control                Vmax - 1/0.35 = 2.9

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