Effect of Temperature on Rate of Reaction of Catalase
Introduction
This investigation was in an attempt to try to find out how varying the temperature can affect an enzyme. The enzyme used was catalase which breaks down Hydrogen Peroxide, this gives off water and oxygen as effervescence. This effervescence is what is used to measure the reaction rate of the catalase. The optimal heat for enzyme activity is proven to be 37oC as anything above this denatures the enzyme. Denaturing is where the heat energy of breaks down the di-sulphide, ionic and hydrogen bonds that hold the tertiary structure together, this in turn changes the shape of the active site and so halts any reactions that the enzyme
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This is why the reaction rate rose with the temperature, however after a certain point (40oC), the enzymes were becoming denatured and this caused them to become useless which is why the reaction slowed to a halt after this temperature.
This was a poor experiment because:
The potato chips were very hard to get exactly the same. This inaccuracy caused the surface area to differ between chips, which means that a small linear error will make a big surface area error. To counter this, a machine should be used to cut the chips to a preset size and would be very accurate. Measuring effervescence was very inaccurate. The Bubbles tended to burst when they were made which caused the overall amount of bubbles to be inaccurate. To prevent this, a syringe could be used or the gas bubbled up through water to get an accurate measure of the amount produced. The temperature of the potato chip when it was placed into the substrate, this means that the enzymes may still be working while they are being heated to the desired temperature, so if the temperature was 80oC then the enzyme may work hard for the first minute or so because the potato is still heating up when in fact 80oC SHOULD cause the enzyme activity to become nil. This probably accounted for some anomalies we received after doing this
The use of multiple test tubes and Parafilm was used for each experiment. Catechol, potato juice, pH 7 phosphate buffer, and stock potato extract 1:1 will be used to conduct the following experiments: temperature effect on enzyme activity, the effect of pH on enzyme action, the effect of enzyme concentration, and the effect of substrate concentration on enzyme activity. For the temperature effect on enzyme activity, three test tube were filled with three ml of pH 7 phosphate buffer and each test tube was labels 1.5 degrees Celsius, 20 °C, and 60 °C. The first test tube was placed in an ice-water bath, the second test tube was left at room temperature, and the third test tube was placed in approximately 60°C of warm water. After filling the test tubes with three ml of the
Students will be observing normal catalase reaction, the effect of temperature on enzyme activity, and the effect of pH on enzyme activity in this experiment. The enzymes will all around perform better when exposed in room temperature than when it is exposed to hot and cold temperatures. This is based on the fact that the higher the temperature, the better the enzymes will perform, but as the temperature reaches a certain high degree, the enzymes will start to denature, or lose their function.
pH - Enzymes also have an optimum pH level. The pH of a solution affects the enzyme's secondary and tertiary structures. These bonds make the shape of an enzyme's active site. So, if these bonds are broken, the shape of the active site changes and is distorted. If there is no active site, there is no reaction resulting in no products. If the enzyme is put in a pH that is very different from the optimum pH, it can cause the enzyme to denature.
As the temperature increases, so will the rate of enzyme reaction. However, as the temperature exceeds the optimum the rate of reaction will decrease.
Using different sizes of potato could show us whether the concentration of enzyme affect the rate of reaction. However, this would not be a practical independent variable as the S.A to volume ratio would not be proportional and the size of the potato to get significant results would be very hard to change. It would be very hard to cut the potato tubers to exact measurements and that could lead to the results becoming inaccurate. An option could be to cut the potato tube into small 1 cm bits and pile then up on top of each other in the test tube, but this again would prove to be impractical as then not all of the surface area of the potato would be exposed to the substrate and this would make my results unreliable. It may also prove to be impractical as having the tuber bits piled on top of each
Temperature can affect the reaction of catechol oxidase by speeding up or slowing down the reaction. I was able to see what happened to the absorbance after changing the temperature of the catechol oxidase solution. I did this by heating and cooling the solutions to measure the absorbances in hot, cold, warm, and room temperature. Then the data was compared to see how the temperature effected the solution. The catechol oxidase solutions reacted best in room temperature (twenty-three degrees Celsius) and the worst in the cold (zero degrees Celsius). I concluded that temperature really does affect the way catechol oxidase reacts.
These results show how temperature of extreme high, or low affects enzyme activity. The highest rate of enzyme activity occurred at 37 Cº. Anything that was hotter or cold than 37 Cº slowed the reaction rate. As I thought, 100 degrees would denature the enzyme, and that was the case. The data provided shows exactly what temperatures enzymes work best, and worst. The objective was achieved as we discovered the different reaction rates under different temperatures. The results are reliable, as we know enzymes do not work well when under extreme heat or denaturation occurs. What I learned in this experiment was that enzymes don’t work well under cold temperatures because they tend to move slower. My hypothesis did not quite match, because I thought they work best at lower temperatures.
The hypothesis tested in this experiment was, if the temperature of enzyme catalysis were increased, then the reaction rate would increase, because enzyme-catalysis reacts by randomly colliding with substrate molecules, and the increase in temperature increases the speed of collision or reaction rate. The final data collected for the experiment was positive with my hypothesis. The coffee filter, covered in potato solution, sank and rose at a faster pace in the hydrogen peroxide when the temperatures were raised.
The null hypothesis for the first experiment was that substrate concentration would have no effect on the reaction rate. It was hypothesized that the reaction rate would increase with rising substrate concentrations, until all active sites were bound. The null hypothesis for the second experiment was that temperature would not have an effect on reaction rates. It was hypothesized that until the enzyme is denatured, as temperature increased, so would the reaction rate.
Between 36.7°C and 4° C there was a decrease in reaction rate. This is majorly due to the fact that less enzyme-substrate complexes are formed as the kinetic energy is decreased and both the catalase and hydrogen peroxide have less collisions with one another (“The Kinetic Molecular Theory”). A temperature decrease would have also caused the molecules to be more tightly packed together, thereby reducing the flexibility of catalase, making enzyme-substrate complexes less likely to occur.
An enzyme also known as a protein, is a biological catalyst which speeds up chemical reactions by lowering the activation energy to increase the rate in which the reaction occurs. The enzyme used was amylase, which breaks down starch molecules into maltose. PH, substrate concentration, salt concentration, and temperature. When enzymes reach a low temperature, the activity is slowed down of molecule movement, but the enzyme is not destroyed. Once enzymes are placed in optimal temperatures once again, it will restore its activity to a normal rate. When enzymes reach too high above optimal temperature, the enzyme is denatured and cannot be restored. In the experiment performed the activity of breaking down starch in fungal and bacterial amylase was being tested at a range of temperatures and time. The fungal and bacterial amylase work best at optimal temperature. Amylase will function best at sixty degrees Celsius at 10 minutes when starch had been one hundred percent hydrolyzed. Hydrolyzed is the breakdown of molecules through addition of water. The experiments independent variables were the time, temperature and enzyme used. The dependent variable was the enzyme activity that broke down the starch into maltose. The controlled variables were the temperature baths, the iodine drop amount, the mixture drop amount, and location of experiment. The control group was the zero minutes without amylase at
Our team was given the temperature of 37 degrees celsius. For this experiment we will be looking for any bubbles and measuring air change in a submerged cylinder. Our hypothesis stated: “At 37 degrees celsius the enzyme would have affected the catalase
reaction rate increases. If the temperature of an enzyme gets to high the reaction rate will slow
Enzymes, proteins that act as catalysts, are the most important type of protein[1]. Catalysts speed up chemical reactions and can go without being used up or changed [3] Without enzymes, the biochemical reactions that take place will react too slowly to keep up with the metabolic needs and the life functions of organisms. Catecholase is a reaction between oxygen and catechol [2]. In the presence of oxygen, the removal of two hydrogen atoms oxidizes the compound catechol, as a result of the formation of water [2]. Oxygen is reduced by the addition of two hydrogen atoms, which also forms water, after catechol is
Enzymes are a key component of a cell. They make chemical reactions happen faster because they lower the activation energy to make the chemical reaction occur. Most of the time, it is best if enzymes produce as efficiently as possible, but in some cases it is better if they do not, when dealing with potatoes (Solanum tuberosum). If the catecholase enzyme of the potato is hindered, it is less likely to brown when it is cooked. To see how efficient sodium chloride is at slowing down these enzymes, the experiment measured the rate of reaction when the enzymes were exposed