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The effect of ph on catalase enzyme
The effect of ph on catalase enzyme
Mechanism of enzymes action in biochemistry
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Discussion
The efficiency of enzymes depends on a number of factors, such as temperature, pH and the concentration of the enzyme just to name a few. This experiment was conducted to show the effects of different pH levels on the activity of the catalase enzyme, the data obtained in this experiment supports the initial hypothesis of the experiment which states that the catalase enzyme will function optimally at a pH of 7 and efficiency will decrease as the pH of solutions moves further away from 7. This is true because in the experiment the test tube containing the distilled water which has a pH of 7, produced the highest amount of foam out of the four test tubes. The efficiency of the reaction can be determined by the amount of foam (foam = oxygen, which is the result of the breaking down of the hydrogen peroxide molecule into water and oxygen) produced, or the level of the fizzing that takes place when hydrogen peroxide is added. The pH of a solution that an enzyme has to function in is very important because if the pH turns out to be too low or too high the enzyme will denature making it unable to function, however, the pH of a solution may be far from the neutral level of 7 but the enzyme might not fully denature which means that the enzyme catalase would not lose its catalytic ability completely whereas a fully denatured enzyme’s shame will have been altered completely causing the active site and substrate to not fit together the way they’re supposed to. In certain reactions, the active site and enzyme substrate are still able to fit together which means that the reaction will continue to take place but at a very low rate, this seemed to be the case in one of the test tubes during the experiment. The foam produced in the react...
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...f denaturing the enzyme, thus making it unable to function because its active site had been reshaped into a shape that did not correspond with the substrate, to allow for them to interlock. The denaturing of the enzyme took place in Test tube B at 7 ½ minutes. The rest of the reactions in the other test tubes were continuing to react. All reactions maintained a very opaque colour and only when the hydrogen peroxide was added to the solution did the contents of the test tube clear up slightly and become more transparent in colour. The transparency of the solutions within the test tubes at the end of the experiment was because of the water that had been produced from the breaking down of the hydrogen peroxide which forms water (H2O) and oxygen (O2). The water diluted the solutions making them more transparent. These results are evidence in supporting my hypothesis.
In the lab, Inhibiting the Action of Catechol Oxidase we had to investigate what type of enzyme inhibition occurs when an inhibitor is added. Catechol oxidase is an enzyme in plants that creates benzoquinone.Benzoquinone is a substance that is toxic to bacteria. It is brown and is the reason fruit turns brown. Now, there are two types of inhibitors, the competitive inhibitor and non-competitive inhibitor. For an enzyme reaction to occur a substrate has to bind or fit into the active site of the enzyme. In competitive inhibition there is a substrate and an inhibitor present, both compete to bind to the active site. If the competitive inhibitor binds to the active site it stops the reaction. A noncompetitive inhibitor binds to another region
The results of this experiment showed a specific pattern. As the temperature increased, the absorbance recorded by the spectrophotometer increased indicating that the activity of peroxidase enzyme has increased.At 4C the absorbance was low indicating a low peroxidase activity or reaction rate. At 23C the absorbance increased indicating an increase in peroxidase activity. At 32C the absorbance reached its maximum indicating that peroxidase activity reached its highest value and so 32 C could be considered as the optimum temperature of peroxidase enzyme. Yet as the temperature increased up to 60C, the absorbance decreased greatly indicating that peroxidase activity has decreased. This happened because at low temperature such as 4 C the kinetic energy of both enzyme and substrate molecules was low so they moved very slowly, collided less frequently and formed less enzyme-substrate complexes and so little or no products. Yet, at 23 C, as the temperature increased, enzyme and substrate molecules
Living organisms undergo chemical reactions with the help of unique proteins known as enzymes. Enzymes significantly assist in these processes by accelerating the rate of reaction in order to maintain life in the organism. Without enzymes, an organism would not be able to survive as long, because its chemical reactions would be too slow to prolong life. The properties and functions of enzymes during chemical reactions can help analyze the activity of the specific enzyme catalase, which can be found in bovine liver and yeast. Our hypothesis regarding enzyme activity is that the aspects of biology and environmental factors contribute to the different enzyme activities between bovine liver and yeast.
Catalase is a common enzyme that is produced in all living organisms. All living organisms are made up of cells and within the cells, enzymes function to increase the rate of chemical reactions. Enzymes function to create the same reactions using a lower amount of energy. The reactions of catalase play an important role to life, for example, it breaks down hydrogen peroxide into oxygen and water. Our group developed an experiment to test the rate of reaction of catalase in whole carrots and pinto beans with various concentrations of hydrogen peroxide. Almost all enzymes are proteins and proteins are made up of amino acids. The areas within an enzyme speed up the chemical reactions which are known as the active sites, and are also where the
When this substrate fits into the active site, it forms an enzyme-substrate complex. This means that an enzyme is specific. The bonds that hold enzymes together are quite weak and so are easily broken by conditions that are very different when compared with their optimum conditions. When these bonds are broken the enzyme, along with the active site, is deformed, thus deactivating the enzyme. This is known as a denatured enzyme.
The shape of the molecules is changing and so the enzyme molecules can no longer fit into the gaps in the substrate that they need to and therefore the enzymes have de – natured and can no longer function as they are supposed to and cannot do their job correctly. Changing the temperature: Five different temperatures could be investigated. Water baths were used to maintain a constant temperature. Water baths were set up at 40 degrees, 60 degrees and 80 degrees (Celsius). Room temperature investigations were also carried out (20 degrees).
Peroxidase activity’s optimum pH was found to be pH 5, since the absorbance rate was the highest at 0.3493. Little activity occurred at pH 3, but the absorbance of the reaction with pH 7 rose steadily to 0.99. The rate of absorbance for peroxidase with pH 9 was 0.0097; pH 9 is incapable of accelerating enzyme activity. This suggests that an alkaline pH is inferior to an acidic pH in increasing peroxidase activity, and that the higher the pH level, the poorer the pH boosts the reaction. A highly acidic pH also reduces
This happens when the temperature is too high; the process is called “denaturing”. When an enzyme reaches a certain temperature, it will have so much energy that it is de-shaped; it is “denatured”. This diagram shows how a denatured enzyme will not work: [IMAGE] The enzymes will hardly work at very low temperatures (they wont be
The Effect of pH on the Activity of Catalase Planning Experimental Work Secondary Resources Catalase is a type of enzyme found in different types of foods such as potatoes, apples and livers. It speeds up the disintegration of hydrogen peroxide into water because of the molecule of hydrogen peroxide (H2O2) but it remains unchanged at the end of the reaction.
Abstract: Enzymes are catalysts therefore we can state that they work to start a reaction or speed it up. The chemical transformed due to the enzyme (catalase) is known as the substrate. In this lab the chemical used was hydrogen peroxide because it can be broken down by catalase. The substrate in this lab would be hydrogen peroxide and the enzymes used will be catalase which is found in both potatoes and liver. This substrate will fill the active sites on the enzyme and the reaction will vary based on the concentration of both and the different factors in the experiment. Students placed either liver or potatoes in test tubes with the substrate and observed them at different temperatures as well as with different concentrations of the substrate. Upon reviewing observations, it can be concluded that liver contains the greater amount of catalase as its rates of reaction were greater than that of the potato.
Investigating the Effect of Substrate Concentration on Catalase Reaction. Planning -Aim : The aim of the experiment is to examine how the concentration of the substrate (Hydrogen Peroxide, H2O2) affects the rate of reaction. the enzyme (catalase).
Purpose: This lab gives the idea about the enzyme. We will do two different experiments. Enzyme is a protein that made of strings of amino acids and it is helping to produce chemical reactions in the quickest way. In the first experiment, we are testing water, sucrose solution, salt solution, and hydrogen peroxide to see which can increase the bubbles. So we can understand that enzyme producing chemical reactions in the speed. In the second experiment, we are using temperature of room, boiling water, refrigerator, and freezer to see what will effect the enzyme.
The Effect of Temperature on the Activity of the Enzyme Catalase Introduction: The catalase is added to hydrogen peroxide (H²0²), a vigorous reaction occurs and oxygen gas is evolved. This experiment investigates the effect of temperature on the rate at which the enzyme works by measuring the amount of oxygen evolved over a period of time. The experiment was carried out varying the temperature and recording the results. It was then repeated but we removed the catalase (potato) and added Lead Nitrate in its place, we again tested this experiment at two different temperatures and recorded the results. Once all the experiments were calculated, comparisons against two other groups were recorded.
The three-dimensional contour limits the number of substrates that can possibly react to only those substrates that can specifically fit the enzyme surface. Enzymes have an active site, which is the specific indent caused by the amino acid on the surface that fold inwards. The active site only allows a substrate of the exact unique shape to fit; this is where the substance combines to form an enzyme- substrate complex. Forming an enzyme-substrate complex makes it possible for substrate molecules to combine to form a product. In this experiment, the product is maltose.
Changes in pH lead to the breaking of the ionic bonds that hold the tertiary structure of the enzyme in place. The enzyme begins to lose. its functional shape, particularly the shape of the active site, such. that the substrate will no longer fit into it, the enzyme is said to. be denatured.