substrate concentration‚ the enzyme is working at “maximum efficiency.” With a concentration at 40‚ it produced 2‚339 products. 2. The maximum velocity of a reaction is reached when the active sites are almost continuously filled. Increased substrate concentration after this point will not increase the rate. The reaction rate increases as substrate concentration is increased. It will soon level off though. 3. When the concentration is at low substrate‚ most of the enzyme molecules are not filled
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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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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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Discussion The primary purpose of this experiment was to determine the optimum temperature range for the activity of the enzyme lactase. Extreme temperatures can have a detrimental effect on enzymes; very hot temperatures can cause the denaturation in the enzyme‚ which is the loss of protein structure. This causes a change in the shape of the enzyme leading to its inability to perform its function. As previously stated‚ the alternate hypothesis read: the optimal temperature range for lactase activity
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Affect of enzyme concentration to the rate of reaction Aim: With the experiment of protein solution‚ in this case egg white added to different pepsin concentrations (0%‚ 0.2%‚ 0.4%‚ 0.6%‚ 0.8%‚ 1.0%) shows‚ as the egg white is a protein and the pepsin works as an enzyme‚ how a higher pepsin concentration and therefore a larger amount of enzymes effect the rate of reaction. Hypothesis: An increased concentration of pepsin speeds up the time the mixture needs to come clear. Introduction:
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Introduction Enzymes are proteins that are involved in all the chemical processes in living things. As they are made of proteins they are affected by pH and temperature. Enzymes are catalysts; they speed up chemical reactions without being changed themselves. Digestive enzymes speed up the breakdown of large food molecules into smaller ones so that the blood can absorb them. Enzymes turn a large starch molecule into thousands of tiny glucose molecules. Enzymes end in ’ase’. There are thousands of
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Effects of Substrate Concentration‚ Reaction Time and Enzyme Concentration on Enzyme Reactions Corey von Ellm-St. Croix Rachael Kwan ID#: 20427841 Matthew Hrycyshyn & Saeideh Mayanloo Biol 130L‚ Section 017 Wednesday‚ 9:30am-12:20pm‚ 151 November 09‚ 2011 A living system controls its activity through enzymes. Enzymes are made from hundreds or even thousands of amino acids connected in a very unique and specific order. Almost all enzymes are proteins‚ except for ribozymes. The chain of amino
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Enzymes are biological molecules (proteins) that act as a catalyst and help complex reactions occur everywhere in life‚ for example a piece of steak that is being digested into energy. Molecules found at the beginning of the process are called substrates‚ and these enzymes exchange them into differing molecules known as products. Nearly all-metabolic processes in a cell need enzymes in order to function at rates that are fast enough to sustain existence. Those who are lactose intolerant are simply
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Received July 18‚ 1997X A radiochemical enzyme assay for studying cyclooxygenase (COX)-catalyzed prostaglandin biosynthesis in vitro was optimized with respect to both COX-1 and COX-2 activity. The assay can be used to assess the relative selectivity of plant-derived inhibitors on COX-1 and COX-2. Assay conditions were optimized for both enzymes with respect to concentration of cofactors (l-epinephrine‚ reduced glutathione‚ and hematin)‚ activation time (enzyme and cofactors)‚ reaction time‚ and
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The environmental factors that effected the rate of enzyme reactions were the enzyme concentration‚ pH‚ and temperature. These environmental factors help enzymes break down the poisonous chemicals into harmless substance. When we tested the liver with 2ml of hydrogen peroxide for a normal reaction it showed that it was exothermic. We added more hydrogen peroxide and the reaction rate of the liver was 3. We learned that the catalase is reusable because the liver reacted both times when we put in
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