Conclusion:
As shown in table 2, the data gathered from the experiment supports the hypothesis that the rate of reaction is highest at pH 7.08 because catalase functions the most efficiently in a neutral environment. It can be seen in the data that the mean value of the rate of reaction is highest at the neutral pH. It shows that catalase breakdown higher amount of hydrogen peroxide into water and oxygen in the pH level of 7. As the pH of the solutions decreased or increased from the optimum level (pH 7), the amount of hydrogen peroxide consumed decreased which means that rate of reaction has decreased. These results support the idea that if the solution becomes more acidic than the optimum pH of an enzyme, then the enzymes will
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This experiment has shown that enzymes must have some environmental conditions present to function properly and achieve the highest rate of reaction. With this information, people can successfully perform experiments using enzymes in the industries by making sure that the environmental conditions present are optimum for the enzyme in the reaction so that maximum yield can be obtained.
In order to avoid errors, I took that pre-stocked catalase solution instead of the catalase extract from fruits because if the extract was taken then it would have been hard to know if catalase enzyme is actually present in the extract or not, which would have put limitations in the experiment.
even though errors were avoided, one source of error in the experiment was that I had to grasp tightly to the test tube end after I connect it with biogas censor because there was a chance of opening up of the lid of the gas sensor from the test tube because of the high gas pressure generated in it from the reaction. So, there was likewise a possibility of losing some of the pressure because of not grasping tightly enough at the top. In case if some of the gas pressure had lost from the test tube, the data gathered is not very accurate. Another source of error could be the unequal measurement of the solution of catalase and hydrogen peroxide to each test tubes. If this happened, then the higher concentration of
The results of the three-part experiment provide a deeper knowledge about the factors that influence the rate of the reaction of the enzyme activity and how the factors influence the structure or function of the enzyme.
Lab six requires students to observe the effects of pH and enzyme concentration on catecholase activity. Enzymes are organic catalysts that can affect the rate of a chemical reaction depending on the pH level and the concentration of the enzyme. As pH comes closer to a neutral pH the enzyme is at its greatest effectiveness. Also at the absorbance of a slope of 0.0122 the enzyme is affected greatly. The pH effect on enzymes can be tested by trying each pH level with a pH buffer of the same pH as labeled as the test tube and 1mL of potato juice, water, and catechol. This is all mixed together and put in the spectrophotometer to test how much is being absorbed at 420nm. As the effect on enzyme concentration can be tested almost the same way. This part of the exercise uses different amounts of pH 7-phosphate buffer and potato juice, and 1mL of catechol mixed together in a test tube. Each substance is put in the spectrophotometer at a wavelength set tot 420nm. The results are put down for every minute up to six minutes to see how enzyme concentration affects reaction rate. The results show that the pH 8 (0.494) affects the enzyme more than a pH of 4 (0.249), 6 (0.371), 7 (0.456), and 10 (0.126). Also the absorbance is greatest at a slope of 0.0122 with test tube C that has more effect on the reaction rate, than test tube A, B, and D.
The hypothesis is that catalase activity will increase exponentially with higher concentrations of hydrogen peroxide until all catalase active sites are filled, in which case 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.
Abstract: Enzymes, catalytic proteins that at as catalysis which makes the process of chemical reactions more easily. There are two main factors that actually affects enzymes and their functions which are temperature and pH. Throughout this experiment, the study how pH and peroxidase affects each other and the enzyme was made. The recordings of how the enzymes responded when it was exposed to four different pH levels to come up with an optimum pH which was predicted in the hypothesis and the IRV at the end.
As seen on table 1, the hypothesis in the introduction of this lab has been supported by the procedures. As the temperature varied from catalases optimal of 37° C, the reaction rate of catalase decreased. 37°C had the highest reaction rate of the three, at 3, while 4°C had the middle rate of reaction at 2.5, and 100° C had the lowest reaction rate of 0.5.
From measuring the length/height of the forth suspension produced when catalase was placed in multiple pH environments and temperatures, I found that generally the rate of reaction was at its peak when places in a pH of 7 (neutral) and subsequently began decreasing as the pH approached 1 and also as it approached more basic conditions at pH 14 (see fig. 2). Also the rate of reaction was at around 50℃ and would generally decrease as temperature either increased or decreased (see fig. 3). When the enzyme was placed in neutral conditions (pH 7), the reaction began instantaneously with bubbles beginning to be released from the potato cube (catalase) immediately (see fig. 1). The reaction was occurring at a rapid rate as it began to turn cloudy
The purpose of this investigation is to discover the effect of pH on the activity of catalase, an enzyme which plays the integral role of converting hydrogen peroxide into water and oxygen, and discover which pH level it will work at the most efficient rate (the optimum). The original hypothesis states that that the optimum would be at a pH is 7, due to the liver, where catalase usually resides, being neutral. The experiment consists of introducing the catalase to hydrogen peroxide, after exposure to certain solutions; hydrogen peroxide, water and hydrochloric acids, all containing the adjusted pH, and measuring the height of froth formed, an observable representation of the activity of the enzyme. The final data indicated that
This experiment is designed to analyze how the enzyme catalase activity is affected by the pH levels. The experiment has also been designed to outline all of the directions and the ways by which the observation can be made clearly and accurately. Yeast, will be used as the enzyme and hydrogen peroxide will be used as a substrate. This experiment will be used to determine the effects of the concentration of the hydrogen peroxide versus the rate of reaction of the enzyme catalase.
Enzymes are high molecular weight molecules and are proteins in nature. Enzymes work as catalysts in biochemical reactions in living organisms. Enzyme Catecholase is found on in plants, animals as well as fungi and is responsible for the darkening of different fruits. In most cases enzymatic activities are influenced by a number of factors, among them is temperature, PH, enzyme concentration as well as substrate concentration (Silverthorn, 2004). In this experiment enzyme catecholase was used to investigate the effects of PH and enzyme concentration on it rate of reaction. A pH buffer was used to control the PH, potato juice was used as the substrate and water was used as a solvent.
The purpose of this experiment was to record catalase enzyme activity with different temperatures and substrate concentrations. It was hypothesized that, until all active sites were bound, as the substrate concentration increased, the reaction rate would increase. The first experiment consisted of five different substrate concentrations, 0.8%, 0.4%, 0.2%, 0.1%, and 0% H2O2. The second experiment was completed using 0.8% substrate concentration and four different temperatures of enzymes ranging from cold to boiled. It was hypothesized that as the temperature increased, the reaction rate would increase. This would occur until the enzyme was denatured. The results from the two experiments show that the more substrate concentration,
If the pH level is too acidic or too basic, then the reactivity and reaction rate of which the enzyme catalase breaks down hydrogen peroxide will decrease.
The purpose of this lab report is to investigate the effect of substrate concentration on enzyme activity as tested with the enzyme catalase and the substrate hydrogen peroxide at several concentrations to produce oxygen. It was assumed that an increase in hydrogen peroxide concentration would decrease the amount of time the paper circle with the enzyme catalase present on it, sowing an increase in enzyme activity. Therefore it can be hypothesised that there would be an effect on catalase activity from the increase in hydrogen peroxide concentration measured in time for the paper circle to ride to the top of the solution.
In this lab or experiment, the aim was to determine the following factors of enzymes: (1) the effects of enzymes concentration the catalytic rate or the rate of the reaction, (2) the effects of pH on a particular enzyme, an enzyme known and referred throughout this experiment as ALP (alkaline phosphate enzyme) and lastly (3) the effects of various temperatures on the reaction or catalytic rate. Throughout the experiment 8 separate cuvettes and tubes are mixed with various solutions (labeled as tables 1,3 & 4 in the apparatus/materials sections of the lab) and tested for the effects of the factors mentioned above (concentration, pH and temperature). The tubes labeled 1-4 are tested for pH with pH paper and by spectrophotometer, cuvettes 1a-4a was tested for concentration and cuvettes labeled 1b-4b was tested for temperature in four different atmospheric conditions (4ºC, 23ºC, 32ºC and 60ºC) to see how the enzyme solution was affected by the various conditions. After carrying out the procedures the results showed that the experiment followed the theory for the most part, which is that all the factors work best at its optimum level. So, the optimum pH that the enzymes reacted at was a pH of 7 (neutral), the optimum temperature that the reactions occurs with the enzymes is a temperature of 4ºC or
The independent variable in this investigation is pH. Each individual enzyme has it’s own pH characteristic. This is because the hydrogen and ionic bonds between –NH2 and –COOH groups of the polypeptides that make up the enzyme, fix the exact arrangement of the active site of an enzyme. It is crucial to be aware of how even small changes in the