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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Computer Enzyme Action: Testing Catalase Activity 6A H2O2 is toxic to most living organisms. Many organisms are capable of enzymatically destroying the H2O2 before it can do much damage. H2O2 can be converted to oxygen and water‚ as follows: 2 H2O2 → 2 H2O + O2 Although this reaction occurs spontaneously‚ enzymes increase the rate considerably. At least two different enzymes are known to catalyze this reaction: catalase‚ found in animals and protists‚ and peroxidase‚ found in plants. A great
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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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Danny Fish 10/9/11 Chemical Testing To identify An Unknown The hypothesis tested was that depending on the solution presented‚ which would test positive for one of the following‚ proteins‚ carbohydrates‚ or lipids through use of chemical testing. (Sudan IV‚ Benedicts’ Solution‚ Iodine‚ Biuret’s) . In order to gain more information for the hypothesis‚ one must know how to test for said macromolecule. Each of the above stated molecules has their own individual solution that will in turn identify
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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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Erin Arroyo Lab report June 11‚ 2013 Biology 123 Professor K Title: Scientific Investigation of the Peroxidase Enzyme & Temperature Abstract: In this lab we tested the effect temperature has on the rate of enzyme activity. The way we figured this out was by taking four different temperatures and testing the different absorbance levels they produced every 20 seconds for two minutes straight using a spectrophotometer. The important part of this experiment was the temperature
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Lab report April 14‚ 2013 Abstract: In this article‚ we will experiment on the significant in strength of the enzyme by using three different test tubes and measuring the amount of product they give off. To determine this we are going to test the amount of color absorbance by using a special tool to help us understand our results. We will see how our end results show the effect of the amount of concentration we apply to each test tube. The results would be shown by the support of two graphs
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