Enzyme Peroxidase Essay

Enzymes are proteins that function as catalysts, speeding up chemical reactions by reducing the activation energy. An enzyme binds to a molecule of a substrate while catalyzing its reaction, therefore, converting the reactants to products without being affected (Auriol, Filali-Meknassi, Adams & Tyagi 2849). A number of factors, such as temperature, substrate concentration, and pH concentration affect enzyme activity. The enzyme used in the lab, Peroxidase, demonstrated the capacity to speed up reactions of compounds to shining or colored product that then qualified for the analysis. The enzyme Peroxidase is present in a wide variety of organisms, including plants, animals, and bacteria. The enzyme functions to breakdown hydrogen peroxide (H2O2), one of the byproduct toxins produced during respiration.

            When reacted with substrate, guaiacol, it produces a red-brown dimer, depicting product concentration. The determination of the reaction rates was done by calculating the slopes of the linear proportion of a graph showing time against absorbance values. The pH alters the shape of the enzyme because peroxidase performs best at a slightly acidic pH. Thus, the enzyme peroxidase have ideal pH where it works effectively. Equally, peroxidase reaction rates have specific limits. They cannot drop past zero where there is no reaction and could not speed up past 100 percent. Therefore, when the ratio of substrate too enzyme is 1:1, the reaction is going speedily. However, increase in substrate reduces activity of peroxidase. Finally, increase in temperate increases peroxidase reaction because of the increase in large number of high energy collisions.

Statement of Hypotheses

1. We consider that a higher concentration (2%) of peroxidase, then the speed of reaction would increase.

2. If we change the pH level of the solution, the rate of absorption would be reduced because the protein enzyme would denature and the reaction would not occur speedily

3. If the temperature of the enzyme environment is increased to 35 degrees centigrade, then peroxidase activity will increase because the kinetic energy of molecules increases and collisions between the enzyme and substrate increase, hence leading to a higher chance of reaction.

Works Cited

Allison, Steven D, Adriana L. Romero-Olivares, Lucy Lu, John W. Taylor, and Kathleen K. Treseder. "Temperature Acclimation and Adaptation of Enzyme Physiology in Neurospora Discreta." Fungal Ecology. 35 (2018): 78-86. Print.

Auriol, M, Y Filali-Meknassi, C D. Adams, and R D. Tyagi. "Natural and Synthetic Hormone Removal Using the Horseradish Peroxidase Enzyme: Temperature and PH Effects." Water Research. 40.15 (2006): 2847-2856. Print.

Daas, Amiour S, and L Hambaba. "Effect of PH, Temperature and Some Chemicals on Polyphenoloxidase and Peroxidase Activities in Harvested Deglet Nour and Ghars Dates." Postharvest Biology and Technology. 111 (2016): 77-82. Print.