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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– The effect of substrate concentration on the rate of enzyme activity of Catalase Aim To investigate the effect of substrate concentration (manipulated by increasing concentration of hydrogen peroxide) on the rate of enzyme activity of catalase‚ produced by liver cells‚ on the decomposition of hydrogen peroxide. Introduction Enzymes are biological catalysts that increase the rates of reactions. In an enzyme-catalyzed reaction‚ the substrate binds to the active site and forms enzyme-substrate
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to evaluate absorbance and the reaction rate of an enzyme‚ ’-amylase in starch-iodine solution. We will be testing the relationship between enzymatic reaction affected by temperature and pH. Through the testing the enzyme at different temperatures‚ and different pH levels; it would determine at which temperature and pH level the enzyme worked the most efficiently. Analyzing absorbance of the solutions with spectrophotometery will determine the reaction rate. To test the optimal pH‚ the starch and
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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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Enzymes are globular proteins that are synthesized by the ribosomes in a cell. They act as catalysts during biological reactions; therefore‚ enzymes are able to speed up these reactions without undergoing a permanent change themselves. These proteins are able to do this by lowering the activation energy of a reaction. To add on‚ enzymes require specific conditions under which they can work best. Reactions occur at faster rates when the temperature is higher. However‚ the rate of an enzyme-catalyzed
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Introduction Enzymes are catalytic proteins. The purpose of a catalyst is to speed up metabolic reactions by lowering the free energy of activation or activation energy. Activation energy is known as the amount of energy needed to push the reactants over an energy barrier‚ so that the downhill part of the reaction can begin (Campbell 151). In an enzyme catalyzed reaction‚ the enzyme binds to its substrate‚ which is the reactant an enzyme acts on. In the reactions‚ the enzymes are very specific
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BIO 5 Lab Report: Lactase Enzymes Enzymes are biological catalysts or assistants. Enzymes consist of various types of proteins that work to drive the chemical reaction required for a specific action or nutrient. Enzymes can either launch a reaction or speed it up. The chemicals that are transformed with the help of enzymes are called substrates. In the absence of enzymes‚ these chemicals are called reactants. Enzymes are thought to have an area with a very particular shape. When a molecule of
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and Physiology Enzyme Lab Report Introduction The chemical reaction that is being studied is the hydrolysis of starch. The enzyme that is being studied is amylase. This experiment is looking at the effect of temperature on the rate of the enzymatic hydrolysis of starch. My hypothesis is that the higher the temperature the faster the hydrolysis of the starch would occur. The rationale behind this is that heat is a form of energy
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characterize thermostable β-Galactosidase enzyme‚ which has been explored in various biotechnological‚ industrial‚ medical and analytical applications. The focus of research was not only limited to thermo stability of β-Galactosidase‚ but also to the production of large amount of enzyme in a short period of time. The β-Galactosidase enzyme hydrolyzes lactose into galactooligosaccharides‚ which are suitable for lactose-intolerant people and has a positive effect on the intestinal bacterial microflora
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purpose of this experiment is to study how enzyme activity is affected by environmental conditions. Researchers tested the level of potato extract enzyme activity with 1-11 pH‚ varying temperature‚ catechol solution‚ hydroquinone solution‚ and different measurements of catechol. In Figure 1A and 1B‚ pH levels were tested with potato extract to see how pH would affect the amount of Benzoquinone is formed in the potato. Although it was hypothesized that enzymes would form Benzoquinone better in acidic
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