Effect of the Changes in the Environment to the Functionality of the Enzymes Introduction a. Background In our everyday lives‚ enzymes are used in our bodies‚ and in nature around us‚ to speed up the chemical reactions happening constantly‚ which happens by lowering the amount of activation energy needed to start various reactions. The way this works is by attaching the particular substrate to the active site of the enzyme‚ where it will start to aid the chemical reaction. Then‚ the allosteric
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Enzymes play a vital role in helping our body function. They act as biological catalysts and help speed up reactions that would otherwise take long periods of time to naturally occur. Enzymes help lower the activation energy required for the reactants to reach the transitional state from which then they can form products. However‚ enzymes do not change the free energy of the reaction. Enzyme’s ability to catalyze reactions comes from the shape of the active site on the enzyme. Enzymes are hyper-specific
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Enzymes are catalytic proteins which speed up the rate of reactions. Every enzyme has a specific function – meaning‚ they can only bind to certain substrates. Because these enzymes are proteins‚ they can be denatured. Enzymes can be denatured by many factors‚ such as pH and temperature. This lab was divided into three parts which examined the effects of pH‚ enzyme concentration and temperature on the rate of which enzymes catalyze. The pH is an index of hydrogen ions. In acidic conditions‚ where
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In this lab the peroxidase enzyme is tested in a dormant avocado seed as well as an avocado seed undergoing the process of germination. A gas pressure will be used to test the seeds and see if the peroxidase enzyme is present in either of the seeds. A catalyst is very similar to track spikes. Spikes increase a runner’s speed‚ as a catalyst speeds up the chemical reaction time in a plant. Neither the catalyst nor shoes are changed in these actions. Enzymes are macromolecules that act like catalysts
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Introduction Enzymes are proteins produced by living organisms to speed up the rate in which chemical reactions occur. This process can happen fast‚ slowly‚ or stop the chemical reaction all together depending on the temperature‚ pH and concentration. Catalase is one of the most common enzymes. It is found in living organisms and is used to break down hydrogen peroxide. This must happen because hydrogen peroxide is considered toxic to cells in the body. However‚ when catalase is used it breaks
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Abstract: Enzymes‚ molecules that speed up chemical reactions‚ are specific to one substrate. In this experiment the substrate hydrogen peroxide and the enzyme catalase will be used. The higher the concentration of potato extract‚ or catalase‚ the faster the reaction and the more substrate present will result in a decrease in the time of the reaction. The amount of concentrations of enzymes and substrates are changed to determine if the reaction is further catalyzed by a greater concentration of
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Enzyme Lab: Peter Kuetzing – 10/4/2012 – F Block 1. How does changing the concentration of enzyme affect the rate of decomposition of H2O2? When more enzymes is added the rate of reaction speeds up. In this case‚ H2O2 will produce more O2‚ in return the kpa/min will go up. 2. What do you think will happen to the rate of reaction if the concentration of enzyme is increased to five drops? Predict what the rate would be for 5 drops. I think that the rate of reaction will slightly increase from
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An experiment was run to determine which enzyme (pectinase‚ and cellulase or combinations of the two enzymes) maximizes juice production and would be most cost effective. The proposed hypothesis was if the enzyme‚ pectinase‚ is added to apple juice‚ then the more juice will be extracted than if cellulase were added because pectinase holds the cell wall together and if it is separated apart from each other‚ then the more juice would be able to flow out. The experimental data show that during the ten
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In this lab we tested the effect of temperature has on the rate of enzyme activity. The way we figured this out was by taking four different temperatures and testing the difference absorbance levels they produced every 20 seconds for about 2 minutes straight using a spectrophotometer. The important part of this experiment was the temperature the enzyme concentration was made at. What we got from the experiment was at lower temperature we got very low numbers for the absorbance‚ which gave us a lower
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1. Prepare a lactase enzyme solution by dissolving one lactase enzyme tablet in 200 ml of water in a clean 250 ml beaker. Stir until the tablet has dissolved. Use labeling tape to label the beaker: “Lactase Enzyme Solution.” 2. Prepare a “denatured” enzyme solution by pouring 20 ml of your enzyme solution into a heat resistant tube. The test tube must have the words “Kimax” or “Pyrex” on it. If it does not‚ it is not heat resistant and may break! Use labeling tape to label the test tube: “Denatured
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