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Enzyme exercise is influenced by a variety of elements that include temperature, pH, enzyme concentration, substrate concentration, and inhibitors. In this case, the focus is on pH. Enzymes are commonly most active at optimum pH. Each enzyme has a pH superior which implies that pH optimum differs from one enzyme to the other. Examples of pH optima are as follows: catalase 7.0, Lipase in the pancreas 8.0, trypsin 7.8- 8.7, pepsin 1.5- 1.6, and invertase 4.5. The pH of a solution is typically key to the functioning of an enzyme because it affects the recreation and structure of the enzyme.
In a n experiment determining the effect of pH on enzyme activity ph will be the independent variable while the amount of foam will be the dependent variable. The amount of foam produced would basically be an indication of the level of enzymatic activity. The enzyme in this experiment is catalase which is produced by the liver. Catalase usually mediates the breakdown of hydrogen peroxide to water and oxygen. Pieces of liver would therefore be used as the source of catalase in the experiment. 2% hydrogen peroxide would therefore be added to a measuring cylinder before placing pieces/ cubes of liver after which the resultant volume of foam reached in the cylinder would be recoded. Throughout the experiment, various pH buffers would added to the hydrogen peroxide in order to determine the effect of pH. As such separate pH buffers 4, 7, 10, and 13 would be added to the hydrogen peroxide solution. The volume of foam reached in the measuring cylinder would be recorded at each step.
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