What are amylases? Amylases are enzymes that break down starch or glycogen. Amylases are produced by a variety of living organisms‚ ranging from bacteria to plants and humans. Bacteria and fungi secrete amylases to the outside of their cells to carry out extracellular digestion. When they have broken down the insoluble starch‚ the soluble end products such as (glucose or maltose) are absorbed into their cells. Amylases are classified based on how they break down starch molecules i. α-amylase
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Omar Shbeeb Toothpick Enzyme Lab 9/25/13 Introduction Enzymes are used in all metabolic reactions to control the rate of reactions and decrease the amount of energy necessary for the reaction to take place. They are responsible for the thousands of chemical interconversions that sustain life. Enzymes are referred to highly selective catalysts‚ meaning they speed up the rate of metabolic reactions. To react‚ they need to find a perfect match with a substrate. They converge at a place called an
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The Affects of pH on Peroxidase Enzyme Claire Bell Biology 1130 Jazmen Myers Section 36 Abstract Peroxidase is a turnip enzyme; it is used in the oxidation of hydrogen peroxide to lower activation energy‚ speeding up the reaction. The activity of peroxidase is highly dependent on its environment and most importantly the pH level. Peroxidase has been the focus of many recent studies and is believed to possibly reduce swelling among other things. We conducted an experiment testing
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Biology Digestive Enzyme Experiment “Design an experiment in which you will investigate a digestive enzyme’s effect on digestion” Research Question: To determine the effect of enzyme concentration on the rate of digestion. This will be done by increasing the concentration of the enzyme diastase and investigate its effect on the rate of starch digestion. The rate will be determined by the amount of time it takes to completely digest the powdered starch‚ the complete digestion will be indicated by
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Conclusion…………………………………………………………………………....…….8 Works Cited ………………………………………………………………………………..9 Properties of Enzymes and Competitive Inhibitors. Abstract: Properties of enzymes were found in this experiment and some other factors‚ which affect enzyme activity. Enzymes are catalyst; they catalyze very specific reactions. Results relating to the active site of specific enzymes played a big role while performing this experiment. The purpose of this experiment was to fin how inhibitors affect
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of an enzyme-controlled reaction. How do these factors affect the chemical structure and properties of the enzyme. Many things can affect the rate of enzyme activity. The temperature of the enzyme‚ the pH of the solution‚ the concentration of the enzyme‚ substrate and the product. Also‚ another affector is the number of competitive and non-competitive inhibitors. As I cannot explain them all‚ I have chosen to explain the effect of temperature and also the effect of inhibitors on enzyme activity
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INTRODUCTION OF ENZYMES Enzymes are complex proteins that cause a specific chemical change in all parts of the body (David C. Dugdale‚ 2011). When we understand enzymes we understand cells (Marshall Brian‚ 2001). In many organisms most chemical reactions are catalyzed -when a substance speeds up the rate of a chemical reaction- by enzymes. Each enzyme controls a certain function that happens in a cell. Still each one has its own process and rate that it converts molecules. Studying enzymes shows how chemical
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substrate concentration‚ the enzyme is working at “maximum efficiency.” With a concentration at 40‚ it produced 2‚339 products. 2. The maximum velocity of a reaction is reached when the active sites are almost continuously filled. Increased substrate concentration after this point will not increase the rate. The reaction rate increases as substrate concentration is increased. It will soon level off though. 3. When the concentration is at low substrate‚ most of the enzyme molecules are not filled
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Received July 18‚ 1997X A radiochemical enzyme assay for studying cyclooxygenase (COX)-catalyzed prostaglandin biosynthesis in vitro was optimized with respect to both COX-1 and COX-2 activity. The assay can be used to assess the relative selectivity of plant-derived inhibitors on COX-1 and COX-2. Assay conditions were optimized for both enzymes with respect to concentration of cofactors (l-epinephrine‚ reduced glutathione‚ and hematin)‚ activation time (enzyme and cofactors)‚ reaction time‚ and
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Enzyme Activators and Inhibitors Lucia House AP Biology‚ Block 4 Mr. Trice October 18‚ 2012 Introduction: Metabolism is the totality of all of an organism’s chemical reactions. Chemical reactions occur due to enzymes‚ a substance which acts as a catalyst in driving chemical reactions in order to produce a desired product (Campbell and Reece‚ 2002). A catalyst is usually a protein; however‚ some catalytic molecules counter this generalization. A discovery made in the early nineteen- nineties
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