Activity Of Alpha-Amylase Experiment

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An Investigation into the Activity of Alpha-amylase Enzyme in Relation to Temperature and PH
The role of amylase in plants is the breakdown of starches so that they can be used as energy in the first stages of early growth (wise geek, [B] 2016). Enzymes are extremely efficient natural catalysts that are found in cells, they work by lowering the activation energy of a reaction and providing an alternative reaction pathway. Enzymes are very specific, only catalysing certain reactions and this is due to the determined shape of the enzyme molecule (Male, 2016). Because amylase is an enzyme, however, it means that it acts as a catalyst to hydrolyse carbohydrates. With the use of alpha-amylase the reaction is increased by a number of
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A pH buffer is a substance however that when present in a solution will counteract the changes in pH (Bloomfield and Stephens, 1996). The buffer molecules easily interconvert between acid and basic forms via accepting or denoting protons as the conditions change (Beals et al, 1999). In plant cells these are extremely important as slight changes in pH can slow down or stop the rate of the reaction of an enzyme via changing its shape and denaturing it. All enzymes have an optimal pH in which they work best because the correct pH regulates and keeps stable the hydrogen bonds that bond the substrate to enzymes (Hostmonster, 2016). In the experiment the results showed that the optimal pH for amylase was a pH of 5 as when the temperature was increased the reaction rate slowed down. Looking at different types of literature and research has shown that the optimal pH has given similar results with the amylase working best at a pH of 4-5 (Journal of Biochemistry, 1960). Therefore, when the temperature is increased in the experiment, the enzymes will denature due to changes to its ionic charge. These ionic bonds create the shape of the enzyme that allow it to function now meaning that it cannot breakdown starch anymore (Chaplin, 2014) which can be seen in the indented

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