The aim of this coursework is to investigate the effect of temperature change, on the rate of hydrolysis of starch catalysed by amylase.
I think that as the temperature increases, the rate of reaction also increases, to a point when it dramatically decreases.
On graph 1, you will see a sketch of the graph which I expect to be the result of the experiment.
I think my prediction is correct because the rate of a reaction simply depends on how often and how hard the reacting particles collide with each other.
If the temperature is increased it means there are more particles of reactant knocking about between the water molecules, which make collisions between the important particles more likely.
Enzymes are catalysts and increase the speed of a chemical reaction without themselves undergoing any permanent chemical change. They are neither used up in the reaction nor do they appear as reaction products.
The rate of a reaction increases until all the active site of an enzyme is filled with a substrate or the reaction has reached its maximum rate, or stopped.
The basic enzymatic reaction can be written as follows:
S + E → P + E
SUBSTRATE ENZYME PRODUCT ENZYME
As you can see, when an enzyme is added to a reaction, it reacts with the substrate but also comes back out at the end, it never changes.
The lock and key theory utilizes the concept of an "active site." The concept holds that one particular portion of the enzyme surface has a strong affinity for the substrate. The substrate is held in such a way that its conversion to the reaction products is more favourable. If we consider the enzyme as the lock and the substrate the key, the key is inserted in the lock, is turned, and the door is opened and the reaction proceeds. However, when an inhibitor which... [continues]
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