Determination of the Activation Energy of an Enzyme Catalysed Reaction

963 Words Mar 14th, 2012 4 Pages
Determination of the activation energy of an enzyme catalysed reaction

Introduction
In this practical the aim for this experiment was to find out the catalytic power of alkaline phosphate, as well as the rate of reaction and the activation energy of p-nitrophenol phosphate.
Enzymes are biological molecules that catalyse a chemical reaction. ‘Enzymes work by lowering the activation energy of a chemical reaction making it easier to proceed’ [1]. This allows molecules to have more energy therefore it makes them collide so that product can be formed much quicker. In order for enzymes to work properly the activation energy must be exceeded first.
Enzymes are described as the lock and key complex. They have an active site which is
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Samples at different incubation times (minutes) | Control 1 | Control 20 | 1 | 3 | 5 | 10 | 15 | 20 | Absorbance | 0.006 | 0.009 | 0.030 | 0.058 | 0.174 | 0.414 | 0.568 | 0.593 | Concentration of nmol p-nitrophenol phosphate/ml from the calibration curve | 0.50 | 0.59 | 2.00 | 3.50 | 9.50 | 24.50 | 35.00 | 37.00 |

Rate of reaction= Y2-Y1/X2-X1
10.5/5 =2.1 nmol p-nitrophenol/min/ml

Table showing the absorbance and concentration at 35 degrees centigrade for p-nitrophenyl phosphate Samples at different incubation times (minutes) | Control 1 | Control 20 | 1 | 3 | 5 | 10 | 15 | 20 | Absorbance | 0.006 | 0.028 | 0.067 | 0.134 | 0.173 | 0.302 | 0.415 | 0.611 | Concentration of