Introduction
Enzyme refers to a molecule that is protein in nature and functions as a catalyst to speed up the rate of a given reaction. The understanding of the basic theory of enzyme kinetic is an essential in the understanding of the mechanisms involved in the activity of an enzyme, as well as in selecting the best method of analyzing the enzyme. There are several factors that have an effect on the rate of an enzymatic reaction. These factors include temperature, pH, enzyme concentration, as well as the concentration of the substrate (Worthington Biochemical Corporation, 2013).
The increase or decrease of the level of these factors may increase or decrease the rate of an enzymatic reaction, and the best level at which the enzyme works best is referred to as optimum level. One of the organs in the body that has most of the enzymatic activities taking place is the liver. The numerous enzymes found in the liver help in facilitating the different kinds of biological activities to work at an optimum rate. Extremely low or high levels of pH result in total loss of enzyme activity. The level of pH also determines the stability of enzymes and the optimum pH is necessary for an enzyme to work effectively. This optimum pH value varies in a great way from one enzyme to another. The catalase enzyme has an optimum pH level of 7.0. It thus requires the environment to have a pH of about 7 for it to work effectively. The vinegar that is mostly used in medical laboratories and for cleaning purposes such as baking, cooking, as well as meat preservation, has a pH level 2.4.
The liver employs huge amount of specialized enzymes in breaking down toxic substances in order to make them harmless for the body to process. One of the enzymes in the liver is the catalase enzyme, which is involved in breaking down the toxic hydrogen peroxide into harmless water and oxygen. Catalase enzyme enables the breakdown of hydrogen peroxide to oxygen and water efficient and thus reduces the harm that would be caused by the accumulation of hydrogen peroxide. The enzyme is, therefore, useful in breaking the hydrogen peroxide down to harmless products. Occurrence of this reaction is confirmed by the presence of bubbles that escape creating foam (Scientific American, 2013)
This experiment was aimed at determining the effect of acidic fluid on the enzymatic activity. The experiment used the acidic fluid (vinegar) as the independent variable while the enzymatic activity of catalase enzyme was taken to be the dependent variable.
Research Question
Do acidic fluids have an effect on the activity of catalase enzyme?
Research Hypothesis
Acidic fluids have an effect on the activity of catalase enzyme.
Methodology
The requirements for the experiment were unprocessed and uncooked liver, beakers, a pen, a knife, distilled water, hydrogen peroxide solution and vinegar. Two beakers were labeled using a pen as Distilled Water and Vinegar respectively.
The liver was cut into small pieces using a knife and divided equally into the two beakers. In each beaker, 40 ml of distilled water and blended and the extract kept frozen. In the beaker labeled distilled water, 0.5 ml of hydrogen peroxide added, and the appearance of bubbles observed. In the beaker labeled vinegar, 5 ml of vinegar was added followed by 0.5 ml hydrogen peroxide. The appearance of bubbles was observed, and the observations recorded.
Results
The appearance of bubbles after the addition of hydrogen peroxide was monitored and the presence or absence of the bubbles recorded in Table 1.
Discussion
The liver sample contains catalase enzyme that is necessary in degrading hydrogen peroxide forming water and oxygen. The presence of bubbles in the sample with distilled water indicated production of oxygen from the hydrogen peroxide breakdown. The neutral pH of distilled water is similar to the optimum pH of catalase enzyme, which is pH 7 and, therefore, favorable for the activity of the enzyme. Distilled water did not affect the stability of the catalase enzyme and thus the structural configuration of the active site was favorable for substrate binding. In the beaker that had vinegar, there were no bubbles that were observed. This is due to the acidic property of vinegar which does not provide the necessary environment for the activity of catalase enzyme. The acidic nature of the vinegar may have inactivated the enzyme by destroying the stability of the enzyme (Worthington Biochemical Corporation, 2013). The wrong pH also destroys the right structural configuration for the active site of the enzyme (Adam, 2012). This affects the binding of the substrate on the active site of the enzyme and hence no enzymatic activity.
In conclusion, the experiment supported the hypothesis that acidic fluids have an effect on the activity of the catalase enzymes. It is thus necessary to set the right pH level for an optimum enzymatic activity to be realized.
References List
Adam, S. (2012). Factors affecting Enzyme Activity. Retrieved July 9, 2013, from http://alevelnotes.com/Factors-affecting-Enzyme-Activity/146
Scientific American. (2013). The Liver: Helping Enzymes Help You! Retrieved July 9, 2013, from http://www.scientificamerican.com/article.cfm?id=bring-science-home-liver-helping-enzymes
Worthington Biochemical Corporation. (2013). Introduction to Enzymes. Retrieved July 9, 2013, from Worthington Biochemical Corporation: http://www.worthington-biochem.com/introbiochem/factors.html
