Introduction
Enzymes are protein whose main function is working as a catalyst for different reactions in the body. It only alters the rate of the reaction it being involved in the same reactions. There are several enzymes in the human body each having a specific reaction to catalyze. An example of an enzyme includes salivary Amylase. Salivary Amylase is an enzyme found in the human saliva. It catalyzes the break down of starch into oligosaccharides via the process of hydrolysis. Therefore, its main substrate is starch. Without this enzyme, this metabolism process would be completely slow. Since enzymes are proteins, their functions are ultimately influenced b some factors that are their structure, optimal pH range, change in the active site of the enzymes, temperature and substrate concentration. In this report, I discuss the efficiency of the salivary amylase enzyme when it is subjected to diverse pH solutions.
Methodology
In this experiment, the effect of pH was observed. Initially, 1 mL of acetate buffer (pH 4) and 1 mL 2% unbuffered starch were put in a test tube. After which 2 mL of the enzyme solution was put in a different test tube. The test tubes were then incubated for about 10 minutes in a the water bath at 37 oC. The two solutions were then instantaneously blended. Three drops of the mixture were rapidly siphoned and two drops of the iodine solution were added concurrently onto the first well of the spot plate. That has been the zero minute. After a one-minute interval with incessant incubation, three drops of the mixture were taken again and two drops of the iodine solution were concurrently added onto the second well. That has been the one minute. The step 5 was repeated until a light-yellow colored solution was observed. The final time (t) was noted. The steps 1 to 6 was repeated for the other pH (4, 5, 6.7, 8, 10) using the appropriate buffer. Finally, the reciprocal of time (1/t, min-1) in step 6 versus the buffer pH was plotted and the optimum pH of the amylase was determined.
Discussions
pH has a climax where the enzymatic reactions are at its maximum. An enzyme activity needs a definite level of acidity and alkalinity to work at its best. The pHs higher or lower than the optimum pH makes an enzyme activity slower and reduced. The optimum pH of the enzyme is pH 6.7, which agrees to the rule of pH 6.7-7 as the optimum pH of salivary amylase. The pHs 4 and 5 are too acidic for a fast enzymatic reaction. At pH 8, the enzymes work fast but are slowly being denatured due to much alkalinity. Enzyme activity at pH 10 will have all the enzymes denatured.
In this activity, starch is the one being catalyzed by the enzyme solution. As mentioned earlier, salivary amylase is a type of enzyme that breaks down starch and turns it into maltose, a disaccharide. To test the presence of an enzyme activity between the two, iodine test was performed. In this test, the rate of loss of reactant or increase of product is being observed. Activators and inhibitors also affect the enzyme activity. Sodium chloride was added to the enzyme solution to hasten the reaction and make it more possible. Chloride ions are important in activating the salivary amylase. How does boiling affect the enzyme activity? Boiling increases the temperature, which destroys the proper shape of the enzymes. The enzymes become denatured hindering the activity to be performed.
Conclusion
In conclusion, the experiment highlights the importance of knowing the factors that affect the enzyme activity. Inability to maintain the optimum temperature and pH of a certain enzyme can deter the assurance of accurate and reliable results. Enzymes are very important in the systems of the living and a simple mistake can alter the process.
During the experiment, the required time involved in the experiment should be carefully followed. The laboratory glass wares should be maintained clean to avoid mixing of unwanted chemical that may affect the results.
Work Cited
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