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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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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Broadly speaking‚ enzymes are proteins that is produced to perform as a biological catalyst in chemical reactions. Catalyst are used to increase the rate of a chemical reaction. In this study‚ we performed two different experiments that investigated the effect of varying substrate concentration‚ and the effect of temperature on the rate of Enzyme-Catalase reaction. In experiment one (i.e. the effect of varying substrate concentration on the rate of enzyme-catalase reaction) we tested the hypothesis
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LAB 1: What temperature does the enzyme actually work properly in? (Hypothesis) If the temperature is below 40 but above 20‚ then the liver will show bubbles. If the temperature is raised higher than the optimum temperature‚ then an extreme decline in enzyme activity would occur following by the quick denaturing of the enzyme‚ rendering it is permanently useless. Also about 37°C is body temperature. The liver that was at 25°C had a huge amount of bubbles (a 4 on the scale) and the 0°C
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Abstract The main goal of the enzyme kinetics experiment was to see how the phosphatase-catalyzed hydrolysis of p-nitrophenyl produced p-nitrophenol in the presence of phosphate and fluoride ion inhibitors of various concentrations. The calculated Km constant was found to be 0.22 for all reactions. The Vmax values for each inhibition ion were 0.00986 for the phosphate ion and 0.00436 for the fluoride ion. The inhibitor constant‚ Ki‚ was determined to be 0.0967 for the phosphate ion. The inhibitor
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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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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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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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Effect of pH on Enzyme Activity A piece of Solanum tuberosum (potato) was removed and mixed with distilled water in a blender. The resulting solution was filtered through multiple layers of cheese cloth to filter out the liquid by eliminating any large pieces in the solution. The solution created was catechol. Five different solutions were prepared as blanks with each test tube containing 6.0mL of a different pH (pH 4‚ pH6‚ pH7‚ pH8‚ pH10) of phosphate buffer‚ 1.0mL of the enzyme and 1.0mL of water
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Ayaan Nadeem SBI 4UO-A Tuesday‚ February 27‚ 2013 Ms. Balmer Pineapple Jelly Enzyme Lab Discussion After completing the Pineapple Jell-O Enzyme lab‚ the final results were that the canned pineapple formed the jelly while the fresh pineapple did not. Pineapple In order for this to have occurred‚ there has to be a comparison between fresh and canned pineapple in terms of their physical and chemical properties. The physical properties of fresh pineapple are that it is sweet‚ ripe and raw.
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