What pH the Enzyme Named Peroxidase Works Best At Essay

You may have observed the reaction of naturally-occurring catalase in tissue from either liver of potato. Design an experiment to determine if the amount of catalase varies from tissue to tissue (e.g. 200 g of liver compared to 200 g of potato).

Hydrate the yeast packets in a beaker with 400 mL of distilled water at a 10% concentration. In a 50 mL

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We hypothesized that a medium pH buffer added to the hydrogen peroxide an peroxidase reaction would be the best condition for the enzyme activity due to it being the more neutral than the high, being basic, and low, being acidic, pH.

Catechol, in the presence of oxygen is oxidized by catechol oxidase to form benzoquinone (Harel et al., 1964). Bananas and potatoes contain catechol oxidase that acts on catechol which is initially colorless and converts it to brown (Harel et al., 1964). In this experiment, the effect of pH on the activity of catechol oxidase was conducted using buffers ranging from pH2 to pH10. Two trials were conducted due to the first trial results being altered by an external factor. The results were acquired by taking readings every 2 minutes for 20 minutes from a spectrophotometer and then recorded on to the table. The data collected in the table were then made into graphs to illustrate the influence of pH on the catechol oxidase catalyzed reaction. After analysis, the data revealed that pH did have a significant influence on the enzyme as recorded by absorbance per minute. However, the data was collected was not accurate due to external factors, thus the results are debatable and should be experimented again for validation.

The purpose of this experiment is to learn the effects of a certain enzyme (Peroxidase) concentration, to figure out the temperature and pH effects on Peroxidase activity and the effect of an inhibitor. The procedure includes using pH5, H202, Enzyme Extract, and Guaiacol and calibrating a spectrophotometer to determine the effect of enzyme concentration. As the experiment continues, the same reagents are used with the spectrophotometer to determine the temperature and pH effects on Peroxidase activity. Lastly, to determine the effect of an inhibitor on Peroxidase, an inhibitor is added to the extract. It was found that an increase in enzyme concentration also caused an increase in the reaction rate. The reaction rate of peroxidase increases at 40oC. Peroxidase performed the best under pH5 and declined as it became more basic. The inhibitor (Hydroxy-lamine) caused a decline in the reaction rate. The significance of this experiment is to find the optimal living conditions for Peroxidase. This enzyme is vital because it gets rid of hydrogen peroxide, which is toxic to living environments.

“Enzymes are proteins that have catalytic functions” [1], “that speed up or slow down reactions”[2], “indispensable to maintenance and activity of life”[1]. They are each very specific, and will only work when a particular substrate fits in their active site. An active site is “a region on the surface of an enzyme where the substrate binds, and where the reaction occurs”[2].

We could use the H2O4 because acids will interfere with hydrogen bonds and other IMFs in the enzyme which would denature it, permanently making the enzyme unable to work. The catalase was the enzyme that acted on the product, which was hydrogen peroxide (H2O2). And of course, the hydrogen peroxide, or H2O2, was the substrate and the catalase was the enzyme.Our results seemed to be consistent because once we added the necessary amount that was needed to determine the amount of H2O2 in the solution, the color of the solution afterwards would always be a light, clear brown, as opposed to having various colors and shades each time. This means that we added the correct, proportional amount of potassium permanganate each time. In comparison to the class data, less of our H2O2 was decomposed. For example, for the trial for 30 seconds, 0.6 mL of our H2O2 was decomposed while the average for the class data was 2.22

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Every enzyme has a temperature range of optimum activity from 30°C to 37°C since the rate of reaction is highest (Meihua Zhaoa, Guangming Zenga, & Danlian Huanga, 2014). The temperature ranges outside the optimum temperature the enzyme peroxidase is rendered inactive and inhibited. It occurs because as the temperature changes (increases and decreases) would supply enough energy to break some of the intramolecular attractions between polar groups (dipole-dipole attractions and Hydrogen bonding) as well as the hydrophobic forces between non-polar groups within the protein structure (DaasAmiour & LeilaHambaba, 2015). The forces are changed and disturbed thus causes a change in the secondary and tertiary levels of protein structure (Pierre Bauduin & Touraud, 2006). The active site is altered in its conformation beyond its ability to accommodate the substrate molecules it was intended to catalyze. Most enzymes within the human cells will shut down at a body temperature below a certain value such below 4°C which

In this experiment, the problem question was how does the concentration of an enzyme affect the rate of the enzyme activity? The identified independent variable was the concentration of enzyme (mL). The variable that is affected by the independent variable is the dependent variable which, in this case, is the reaction rate (floating units/minutes). Other variables that stayed unchanged throughout the experiment include the amount of 1% hydrogen peroxide and the room temperature. The hypothesis that was tested in this experiment was if we poured 40 mL of the potato solution (hydrogen peroxidase) into cup 1, then cup 1 will react the fastest because it has the highest concentration of enzymes among the four solutions.

This experiment used beets to determine peroxidase production in stressed plants. The purpose of this experiment was to test if the stressed plant would produce more peroxidase in a higher concentration than the control plant. The stressor for this experiment was watering with salt water. This stressor was chosen because it is a natural stressor to plants; especially along the coasts and where roads are salted in winter such as the Midwest. The control plant was watered with plain tap water while the experimental plant was watered with tap water plus salt. The salt water concentration was 1.2341 molar. After the two-week stress period the stressed plant was much smaller, wilted, and shriveled compared to the control plant. It also had less water content overall, which made the extraction process somewhat more challenging. To test the peroxidase production in the plants several methods were used, including: tissue printing, DOT-blot assay, electrophoretic analysis, and a spectrophotometric assay. It was concluded that the stressed plant did produce more peroxidase than the control plant and in a higher concentration.

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