An Investigation Into the Effects of Temperature on Enzyme Action

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An investigation into the effects of temperature on enzyme action An enzyme is a biological catalyst that speeds up the rate of reaction in certain biological functions. They play a vital role in many aspects of human physiology and are necessary for the functioning of a number of systems, for example in the digestive system to help to break down food. All enzymes have a unique active site that can fit on to a particular molecular arrangement on a target substrate; a substance e.g. carbohydrate, protein, or fat, that the enzyme is designed to breakdown. There are a number of different enzymes in the human body; each type produced specifically to perform a certain role. Enzymes are not themselves destroyed in the reaction to break down a substrate but their effectiveness is reduced under certain adverse environmental conditions. The two most important ones are temperature and PH level; also concentration of enzyme is also a determining factor. Enzyme action is biochemical in nature and, in line with many chemical reactions; it speeds up with an increase in temperature. This would continue until a certain critical temperature is reached where it’s working efficiency drops suddenly. This is due to a deforming or ‘de-naturing’ of the active site leaving the enzyme unable to bond with its substrate. In humans this can have life threatening consequences if the body temperature rises above 40 degrees Celsius. As enzymes normally function in their own particular part of the anatomy, they operate most efficiently in a medium with a specific acid/alkali (PH) balance. If this balance is either too high or too low it’s functioning is reduced and in extreme circumstances this can lead to de-naturing also. An investigation was carried out in order to study the functioning of a particular enzyme ‘Trypsin’. This is produced in the pancreas and is found in the pancreatic juice; it is used to break down proteins. As it is believed that all enzymes function most efficiently at...
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