In this lab the peroxidase enzyme is tested in a dormant avocado seed as well as an avocado seed undergoing the process of germination. A gas pressure will be used to test the seeds and see if the peroxidase enzyme is present in either of the seeds.…
In our experiment we conducted an experiment to validify our hypothesis: “ If the enzyme concentration increases, it would alter the rate of which the color changes.” We hypothesized that the increase of an enzyme concentration would result in the increase of reaction rate; our experiment provided enough data to prove our hypothesis. The function of this experiment was to investigate how the influence of turnip peroxidase enzyme on the rate of reaction. As a given we would have 20g of turnip in 500 mL of deionized water. We would have a three different trials and in those trials we would do it three times.…
For Figure 3, the rate of peroxidase activity greatly increased from the first to second pH, increasing .7 (AU/sec), while the second to third pH increased only .1. On the other hand, the third to final pH decreased, just like the temperature chart (Figure 2) .45 rate of activity.…
Enzymes are biological catalysts or assistants that consist of various types of proteins that work to drive the chemical reaction required for a specific action or nutrient. They can either launch a reaction or speed it up. Catalase is a common enzyme found in nearly all living organisms exposed to oxygen. It is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species (ROS). The catalase used in this experiment will come from five different sources: Spinacia oleracea (Spinach), Brassica oleracea (Broccoli), Solanum tuberosum (Russet Potato), Malus domestica (Apple), and Allium cepa (Onion). The five different catalases from the sources will all be used to catalyze Hydrogen peroxide (H2O2). When hydrogen…
We found a study about the effects of glycosylation and pH conditions in the dynamics of human arylsuffatase A. They concluded that lowering pH and increasing glycosylation reduced the flexibility of the enzyme. Also, at acidic pH levels the glycosylated enzyme had a higher conformational stability. This study was similar to ours in that it investigated how pH conditions affect enzyme functionality. They found optimal pH conditions for the enzyme like we did, but they took into account another variable that is that influenced functionality…
The pGLO lab is a lab where students attempt to put the genes that make a jelly fish glow into E. Coli. After a process called transformation, the process in which a cell takes up and expresses a new piece of genetic information, the E. Coli will be able to glow and will be antibiotic resistant. The students first need to learn a couple of techniques before they are able to begin this lab. The first technique they will need is how to keep their environment sterile. They must learn to only open their tools, and other supplies for as long as they need, and keep them from touching anything. They must also learn that tools can never be shared between specimens, and when they use a tool, they should dispose of it and get a new one. Next they need to learn how to transfer a bacterial colony. To do this, one must use a sterile loop and scrape one colony off of the dish. Then they must insert the loop into…
The enzyme peroxidase has been shown to break down H2O2. Enzymes are known to increase the rate at which a chemical reaction occurs. We looked at factors that affected the breakdown of hydrogen peroxide. These effects are the different temperatures and pH levels the enzymes were placed in. We found that the optimum, or best condition, temperature for the enzymes tested was about 22 degrees Celsius. The optimum pH level for the enzyme was 7.…
If you’ve ever left a cut up apple out for long, you’ll notice that after a while, it will turn brown. The reason for this is an enzyme named catechol oxidase, a ubiquitous plant enzymes containing a dinuclear copper center (Klabunde, Eicken, Sacchettini, & Krebs, 1998). In this experiment, we used two different chelators, ethylene diamine tetraacetic acid and phenylthiourea to test which would stop the effects of catechol oxidase on potato cells by testing the change in absorbency over time. Our data supported our hypothesis that EDTA would have a greater change in absorbency over time than PTU.…
Problem: How can we demonstrate how enzymes work? What happens if we alter the environment of an enzyme?…
To further catalase activity studies, one can compare and contrast other plant species to the potato or keep the potato and change other variables such as the buffer used and/or temperature which has been done by others in the laboratory. Another experiment could be to pinpoint the location of catalase enzymes in an orange fruit.…
Over a two week period of time in the laboratory, we experimented and tested the reaction rate of a peroxidase enzyme and the factors that affected it, both positively and negatively. The purpose of these experiments was to probe and manipulate the activity of the enzyme peroxidase by varying temperature, pH, the amount of enzyme compared to the substrate and the effect of hydroxylamine. Peroxidase activity is expressed when the potato extract is subjected to stresses such as low temperature (El-hilali et al., 2012). The most eye catching factors that we tested for their impact on enzyme activity involved change in pH, temperature, boiling extract, and the effects of probing the active site with hydroxylamine. In the first part of…
This was conducted through four different experiments. The first tested the effect of temperature on enzyme activity. The independent variable in the first experiment was the temperature of the solution of pH 7 buffer, potato juice, and the enzyme. The independent variable for the second experiment was the pH of the phosphate buffer. The independent variable for the third experiment was the enzyme concentration of the solution, and finally the independent variable of the fourth experiment was the substrate concentration.…
To determine the effect of various factors on the rate of reaction between an enzyme and its substrate, and also to determine the optimal ranges under which the enzyme activity is maximized. Also to determine whether saline and alcohol are inhibitors or activators…
To test the effect of a substrate concentration on enzyme activity, the amylase enzymes were combined with a different substrate concentration (starch) and the rate of the reaction was determined with the aid of I2kI. If starch was detected, the solution turned to dark blue; if the starch was already broken down, then reaction stayed colorless. To test the optimal PH, the starch and a buffer were combined at a specific PH level and the rate of reaction was tested. To determine the optimal temperature of amylase enzyme, the solution and amylases enzyme were held at various temperatures and the rate of reaction was determined.…
Kartinen (2012), it is tested whether or not the amount, or concentration, of catalase enzyme directly affects its reaction rate. His hypothesis was that the highest concentration would show the fastest reaction time. Kartinen extracted catalase from potatoes by peeling, cutting, and blending them. The extract was then used for make solutions of different concentrations or percentage. After coffee filters were soaked in the solutions, they were put into the substrate, hydrogen peroxide, and timed for how long they took to rise. This would be the reaction rate. As Kartinen expected, the concentration of 100% was fastest, 90% second-fastest, and so on. This happened due to the pH of the solution and how it affected the reaction time. In conclusion, the pH had to be at balance with the reaction time, as it was with the 100% concentration and not far behind with the 90% and 80% (Kartinen…