The effect of Temperature on the rate of Enzyme Activity.

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Farah Aslam

Biology Practical Assessment:

The effect of Temperature on the rate of Enzyme Activity.

Interpretation of Results:

Table to show the effect of temperature on the rate at which rennin solidifies the milk protein caseinogen.

Anomalies*

Trends and Patterns:

Up until 60ºC, the general trend of the graph shows that as the temperature increases, the rate at which the milk solidifies increases. When the temperature was at 49ºC, the rate was highest but above this the rate decreased until it reached 0 at 60ºC.

Between 35 and 39ºC, the rate increased from 4.4/s-1 x1000 to 7.5/s-1 x1000. However, between 39 and 44ºC the rate did not increase as much and this is shown on the graph as the gradient between these points is not as steep as between 35 and 39ºC. Between 44 and 49ºC there is a sharp increase from 9.2 to 13.9/s-1 x1000. Furthermore, between 49 and 60ºC the rate decreases at an even greater rate as indicated by the steepness of the graph at these points where the rate decreased from 13.9/s-1 x1000 to 0/s-1 x1000.

Conclusion:

The graph shows that the highest rate at which the milk protein is solidified by the rennin is 13.9/s-1 x1000 and this occurred when the thermostatically controlled water bath was set at 49ºC. Therefore, based on this graph, we can say that the optimum temperature for the enzyme rennin is 49ºC. Consequently, above this temperature, the graph shows that the rate begins to decrease and so this indicates that at his point, the shape of rennin’s active site is altered, causing the enzyme to denature.

Discussion:

Enzymes are biological catalysts and speed up chemical reactions by reducing the activation energy required to break the bonds in the reactants in order to form the new products.

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All enzymes are globular proteins, each with a specific three- dimensional tertiary structure that determines its function. Enzymes are usually specific to the substance- or substrate- they work with and so the shape of the enzyme’s active site- where the substrate binds - has to be complementary to the shape of the substrate.

In the case of this reaction, the enzyme (rennin) is catalysing the breakdown of the substrate (milk protein- caseinogen)

Whether it is induced fit or the lock and key which occurs, the ...

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