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Important of enzymes
Important of enzymes
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Because of the fact that reactions are catalyzed by enzymes when they randomly collide with substrate molecules, increasing the temperature would increase the reaction rate. Increasing the temperature further increases the vibrational energy of the enzyme molecules, straining the bonds that keep them together. Furthermore, when the temperature is higher, more bonds will break because of these strains, causing the active site of the enzymes to change too. Similar to pH, a change in the shape of the active site leads to the substrate not being able to fit perfectly, leading to the enzyme not being able to catalyze the reaction. Overall, an increase in temperature will cause the rate of reaction to increase initially due to the increased kinetic energy.
Catalase Activity on Substrate Based On Gas Pressure Production Rate Name of the Class Author’s Name Date Enzymes are organic compounds which act as catalysts and speed up biological reactions in biological organisms. They are not destroyed or changed during the reaction but rather they are used over and over again to catalyze many more reactions. Their activity may be affected and altered by factors such as temperature, substrate concentration, enzyme concentration and Ph.
The objective of this lab was to determine the best pH level to increase enzyme activity. As this objective was met, it was discovered that water (pH level 7) was the best for percent absorbance. The hypothesis for this experiment was, “If peroxidase is an enzyme and therefore contains certain pH tolerances, then when placed in solution with pH levels of three, seven, and ten and the reaction is measured by a colorimeter, then water will be the optimal solution for maximum reaction rate.” As seen in the tables and graphs, the data supported the hypothesis due to the fact that most enzymes have an optimal pH of 4-9.
We also tested to see if Peroxidase was able to recover its catalytic ability after being exposed to sub optimal temperatures. After being brought to optimal temperatures the solutions were still able to react,
The effect of pH on the speed of enzyme interaction with substrate chemicals Hypothesis: About pH: If the pH level is less than 5, then the speed of the enzyme reaction will be slower. About temperature: If the temperature stays the same, then the speed of the enzyme reaction will not be completely affected. Background information: The function of enzymes is to speed up the biochemical reaction by lowering the activation energy, they do this by colliding with the substrate.
Enzymes speed up chemical reactions enabling more products to be formed within a shorter span of time. Enzymes are fragile and easily disrupted by heat or other mild treatment. Studying the effect of temperature and substrate concentration on enzyme concentration allows better understanding of optimum conditions which enzymes can function. An example of an enzyme catalyzed reaction is enzymatic hydrolysis of an artificial substrate, o-Nitrophenylgalactoside (ONPG) used in place of lactose. Upon hydrolysis by B-galactosidase, a yellow colored compound o-Nitrophenol (ONP) is formed.
(Enzymes par. 1) They are very sensitive to their surroundings and highly reactive to the pH levels and temperature once exposed to either one. Temperature causes damage to the enzyme,
Introduction Chemical reactions are seen in many instances, including those in which one substance is being converted to another. Natural chemical reactions will occur without intervention, however they occur slowly. Enzymes become important in these situations. Enzymes are proteins that act in cells to ensure reactions occur at appropriate speeds. In other words, they act as catalysts.
The fungal amylase showed the highest enzyme activity was at this temperature, with the lightest color from all the temperatures. Thus the individual group data, showed bacterial amylase to have an optimal temperature at 0°C, and fungal amylase showed to have an optimal temperature at 55°C. Nevertheless, the class data does not support these findings by the individual group. Base on the class data, both bacterial amylase and fungal amylase have an optimal temperature of 55°C, proving the hypothesis. This difference between the class data and the individual data shows that errors must have occurred while preforming the bacterial enzyme
We use peroxidase as our enzyme in the experiment. Peroxidase is found in plants, such as turnip, and can convert hydrogen peroxide to water and oxygen. We had which were hydrogen peroxide (3%) and hydroxylamine. The hydrogen peroxide competes with the hydroxylamine for the active site molecules from peroxidase. The peroxidase needs the hydrogen peroxide in order to separate it into water and oxygen.
Results Figure 1. Effect of temperature on the reaction rate between catalase and H2O2 Figure 1 shows that the optimum temperature for catalase to catalyze hydrogen peroxide is around room temperature (30℃) as it has a very fast reaction rate (5). The overall trend is that temperatures that differ from 30℃, will decrease the reaction rate. Discussion This experiment supported the hypothesis, since catalase was the most effective with hydrogen peroxide when it was in an environment with a temperature of 30℃.
A simple change in temperature, a molecule out of place, and a sudden change in the pH level are just some of the things that can harm an enzyme 's reaction rate (the speed at which a chemical reaction proceeds) (5). To test the reaction rate of an enzyme, a lab was done to simulate what would happen to an enzyme under extreme conditions. The enzyme (represented by a hand) had to catalyze as many substrates as possible (represented by toothpicks) within 60 seconds. The experiment dealt with environmental factors such as extreme cold, presence of other molecules, etc. The lab that was simulated directly correlated to many of the topics discussed in class, like explaining the importance of enzymes and measuring the enzymes’ ability to function under different conditions.
Research question What is the effect of temperature Amylase activity? Word count-1453 Background research Enzymes are biological catalysts that speed up a chemical reactions. They do this by decreasing the activation energy(the energy needed to start the reaction) of a chemical reaction. The enzyme present in our saliva is called Amylase. Amylase increases the rate of reaction by decreasing the activation energy needed to hydrolyse the starch molecules.
They can only quicken reactions that will eventually occur, but this enables the cell to have a productive metabolism, routing chemicals through metabolic pathways. Enzymes are very specific for the reactions they catalyze; they make sure the chemical processes go in the cell at any given time. Peroxidase was the enzyme being testing in this experiment. A peroxidase is an enzyme that acts as catalysts, which occurs in biological systems. Peroxidase is found in plants, which they play a role in helping to minimize damage caused by stress factors or insect pests.
1. The reaction is an oxidation and reduction reaction. Bubbles were observed because oxygen is being release from the reaction as a gas as part of the reduction part of the reaction. Enzymes work efficiently at a body temperature of 37o C therefore if the enzyme was boiled before adding it to the peroxide there would be no bubbles due to the fact that the enzyme would be denatured.