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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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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Enzymes are proteins that increase or decrease the rate of chemical reactions. They are generally globular proteins and are around 62 amino acids residues in size. What enzymes do is determined by their 2-dimensional shape. A lot of enzymes are bigger than the substrate they act on‚ but only a little part of the enzyme involved directly with the catalysis. Without enzymes the chemical reactions in the body‚ would be so slow‚ the body would shut down. And cell reactions would take too much energy
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Effect of Temperature on Enzymes ~Abstract~ In this experiment the effect of different types of temperatures on enzyme activity was examined. The temperature baths that were used to test the difference in enzyme activity on fresh liver were; 4 °C‚ room temperature which was 22°C‚ body temperature which is 37°C‚ and 77°C. The total time of each trial was 2 and a half minute‚ 1 minute for the H2O2 to acclimatize to the temperature‚ 1 and a half minutes for the reaction to occur. Catalase causes Hydrogen
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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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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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