The Effect of Temperature on Enzyme Activity and Oxygen Production Throughout this report you will gain information as to how temperature effects the amount of oxygen produced in an enzyme- catalase experiment. In the experiment we used liver extract as a catalase and created a chemical reaction within a reaction chamber between the catalase and hydrogen peroxide as well as three different controlled temperatures. In the procedure below there will be a step by step process as to how
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Enzyme Lab Using Jello INTRODUCTION: Enzymes are known as protein catalysts. The name protein catalyst suggests that most enzymes are made of proteins. A catalyst is a substance that speeds up chemical reactions without being consumed in the process. (Giuseppe‚ M 2002‚ p.69). After a reaction has been catalyzed‚ the catalyst can be used again to catalyze the same reaction. Enzymes reduce the activation energy (minimal energy) it takes for a reaction to take place. Enzymes can either catabolize
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hydrogen peroxide and potatoes (enzymes)? Introduction The enzyme used for this experiment is Catalase. Catalase is inside mostly any living organism which uses oxygen. Its job is to break down hydrogen peroxide‚ into oxygen and water. (Formula) 2H2O2 ---> 2H2O + O2 (lab manual). There are limiting factors which if altered‚ can alter the procedure of the reaction‚ such as temperature‚ pH‚ and the concentration of either the enzyme or the substrates. Enzymes are specialized class of protein
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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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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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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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Horseradish Peroxidase Abstract There are several factors that can affect the rate of reaction of peroxidase such as temperature‚ pH‚ concentration of peroxidase present and whether or not it has been boiled. Our experimental data demonstrated that peroxidase activity peaked between 23 degrees Celsius and 32 degrees Celsius. We found the pH to be 7 for optimal activity. As far as the concentration is concerned our results showed that as the concentration of horseradish peroxidase doubled so
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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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