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Recommended: Catalase activity
At the time of conducting the experiment, the intention was to analyse the effect that an increase in catalase concentration had on the amount of oxygen (O2) produced if the hydrogen peroxide (H2O2) concentration was constant. It was proposed that when the catalase increases in concentration at the increments of 0.5%, 1%, 2%, and 4% and the hydrogen peroxide remained at a fixed concentration, the oxygen production would rise gradually. It was suggested that this would occur due to the collision theory ("BBC - GCSE Bitesize: Collision Theory") and the greater number of active sites thus an increase in accessibility allowing enzyme- substrate complex’s to be formed. According to the data gathered from the experiment, it can be implied that the hypothesis was supported as the data indicates an incline in oxygen …show more content…
This is evident as the average gradient for 0.5% catalase concentration is 0.067%/s and the average gradient of 4% catalase concentration is 0.315%/s. The rise of oxygen production has occurred because as the hydrogen peroxide is added to the varying levels of concentration of catalase. The solution with the highest enzyme concentration will yield the most activity, thus producing more oxygen gas ("Enzyme Investigation. How Does The Concentration Of Hydrogen Peroxide Affect The Amount Of Oxygen Produced By The Enzyme Catalase? - International Baccalaureate Biology - Marked By Teachers.Com"). This assumption is based on scientific theory, which states an increase in enzyme concentration will also increase the chances of substrate-enzyme binding.("General Principles - Chemwiki") An example of this is the average R2-value for 1% catalase solution was 0.090%/s and the average R2- value of the 2% catalase solution was 0.094%/s. This indicates a strong positive correlation, meaning that as x increases (catalase concentration), y also increases (rate of oxygen
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
The purpose of this study is to analyze the activity of the enzyme, catalase, through our understanding
In both solutions of catalase there is a steady increase in reaction relative to the hydrogen peroxide concentration as it increases. A significant jump is observed in the carrot catalase solution between .25% and .5% whereas the pinto bean catalase solution has a steady increase. Each solution doesn’t generate much more reaction to the next increment of hydrogen peroxide concentration, 1%. In general it stayed level. This continued to be a trend for the pinto bean catalase solution, plateauing through to the 6% concentration of hydrogen peroxide. This is known as the point of saturation.
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
How does the temperature (-2°C, 20°C, 30°C, 40°C, 60°C) affect the production of oxygen (cm3) from cow hepatic (the enzyme catalase) when placed in boiling tube with 10 ml of 3% hydrogen peroxide for 1 minute?
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).
Hydrogen Peroxide does not need the enzymes in the catalase to separate into Oxygen and Water. The catalase are only used to increase the rate of reaction.
Investigating Factors that Affect the Rate of Catalase Action Investigation into the factors which affect the rate of catalase action. Planning Aim: To investigate the affect of concentration of the enzyme catalase on the decomposition reaction of hydrogen peroxide. The enzyme: Catalase is an enzyme found within the cells of many different plants and animals. In this case, it is found in celery.
Because of its undeniable and scientifically-proven powerful antioxidant properties, catalase enzyme has a wide commercial application. Primarily in combination with the enzyme glucose oxidase, catalase is used as a preserving system in mayonnaise and egg products such as whole eggs or dried egg white, in the preparation of milk and cheese, in the manufacture of baked goods, beverages, textile industry, cosmetic industry (as face mask), and in cleaning agents for contact lenses, for the elimination of the hydrogen peroxide that is present in some products, (Worthington Biochemical Corporation,
This is because there is more hydrogen peroxide to be broken down by the enzyme and with more hydrogen peroxide in the reaction, more oxygen is released.
The enzyme will drastically slow down activity due to cold temperatures of 24°C. Just like the energy stored in human and plant organisms. If cells are under a certain temperature within living things, the ability to function will not hit equilibrium but will slow down the rate of chemical reaction. It is clear that room temperature is where we will see most of the activity. This is part of the reason why homeostasis is important to living organisms – because homeostasis is the process to maintain internal temperatures so that the structure and function can work properly. The catalase enzyme vs. hydrogen peroxide delivered clear results that environmental factors can alter enzyme activity. That being said our hypothesis was accepted based on the prediction that heat will denature the enzyme while the activity of cold and room temperatures will still have a reaction. This hypothesis could have wrong if other factors were involved such as, if we let them sit for a long period of time or if there were more temperatures involved. In conclusion, later on we may want a larger form of data by including the class results but as of now this experiment went well and confirmed our
Aim: in this experiment is to use this reaction to see what substances have high levels of the Catalase enzymes and if different acids and basses are added would affect the reaction and the enzyme.
Without enzymes, reactions wouldn’t occur and living organisms would die. For instance, the enzyme in the stomach breaks down large molecules to smaller molecules to absorb nutrition faster. Researchers experimented with enzyme activity with a potato extract. Researchers will test enzyme activity by increasing and decreasing pH levels, lowering and increasing temperature, and substrate concentration effects. In the first experiment, researchers hypothesized whether different pH levels would change how much Benzoquinone are created and how will the enzymes function in neutral pH levels than higher and lower levels. Researchers used potato extract and different levels of pH to test their hypothesis. In addition, researchers questioned at what temperature does the greatest amount of potato extract enzyme activity take place in. Researchers then hypothesized that the results would indicate the greatest amount of potato enzyme activity level will take place in room temperature. In this experiment, researchers used potato extract and different temperature levels to test the hypothesis. Moreover, researchers wanted to test the color intensity scale and how specific catechol oxidase is for catechol. In this experiment, researchers used dH2O, catechol solution, hydroquinone, and potato extract. Lastly, researchers tested the substrate concentration and how it has an effect on enzyme activity. In this experiment researchers used different measurements of catechol and 1cm of potato extract. Researchers hypothesized that the increase o substrate would level out the enzyme activity