Investigating the effect of changing substrate concentration on the activity of the enzyme catalase The aim of this experiment is to examine how the concentration of a substrate (hydrogen peroxide) affects the rate of reaction of an enzyme catalyse (found in liver cells) Research Question: how does changing the concentration of the substrate affect the rate of reaction of the enzyme catalyse? Hypothesis: As the concentration of the substrate increases‚ so does the rate of reaction until the reaction
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however‚ without enzymes‚ these reactions could possibly take several years to complete. An enzyme is a macromolecule‚ generally a protein‚ that lowers the activation energy of a reaction without being changed by the reaction‚ and this causes the reaction to occur much faster than usual (Campbell et al.‚ 2014). The act of speeding of a chemical reaction is called catalysis‚ and molecules that perform this are called catalyst. Enzymes act as catalysts‚ and there a many types of enzymes that perform many
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reaction. Life would not exist without the presence of enzymes (Phillips‚ 2017). Through chemical reactions‚ this energy is created and is controlled by a catalyst‚ enzymes. Enzymes are known as proteins that are produced in living cells that speed up the metabolic processes of an organism. These catalysts speed up these reactions by decreasing the activation energy‚ how much energy is needed for a chemical reaction to happen (WBC‚ 2015). An enzyme-substrate complex forms when a substrate attaches to
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relationship between substrate concentration and initial reaction rate provided that substrate concentration is much greater than enzyme concentration. Enzymes are essential to life as they are required for many vital metabolic reactions to occur. To adequately explain the properties of enzymes‚ it is assumed that an enzyme-controlled reaction takes place through an enzyme-substrate complex by the lock and key mechanism. It is hypothesized that a greater concentration of product is achieved through
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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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Explore Download 0CommentLinkEmbedof 6Readcast0 inShare Xavier Bourret-Sicotte Physics18/09/2007 Measuring the speed of sound In this experiment‚ we will measure the speed of sound.The apparatus consisted of a plastic tube filled with water linked to a water container. Thiscontainer could be displaced vertically in order to change the water level. We would thenmake a tuning fork vibrate above the pipe and change the water level until the resonance wasat maximum intensity.Hypothesis: The
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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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