Alpha Amylase Experiment

An Investigation into the Activity of Alpha-amylase Enzyme in Relation to Temperature and PH
Introduction:
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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In a similar experiment done by a student (UK Essays [B], 2015) they also discovered that the optimal temperature was between 30oC and 40oC and they also made the statement that 37oC would have been optimal but no results were gained from this temperature so claim can be made, many other experiments also claim that 37oC is the optimal temperature. The reason that the temperature has this effect on the reactions is because of particle collision theory. An increase in temperature causes the enzymes and the substrates to collide more frequently as they have more energy therefore increasing the reaction rate. When the temperature exceeds its optimum the active site denatures, slowing down or stopping substrate binding and hating the reaction (Kopaleishvili, 1995). At lower temperatures, the energy of particles is lower and there are less collisions. Therefore, at 0oC the particles were barely colliding as they had reduced energy and the hydrolysis of starch took longer than 24 minutes, however. At 20oC the enzymes are gaining more energy and they are colliding more until they reach the optimal amount of energy per particle at 40oC and are reacting the fastest. At 80oC the enzymes are denatured as the polypeptide bonds are broken. This is irreversible and the amylase is then useless, however at the other …show more content…
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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