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 (alpha-amylase)
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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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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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Stallings Period 2 January 26‚ 2013 Enzyme Catalysis Lab Report Background: Enzymes are catalyst‚ which affect the rate of a chemical reaction. One consequence includes the cell to carry out complex chemical activities at relatively low temperatures. In these reactions the substrate binds reversibly to the active site. The cause of this is a decrease in the energy needed to activate the reaction of the substrate molecule to from products. Every enzyme is particular for a reaction for the reason
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three different Substrate Concentrations (3%‚ 1% and 0.3%) as which one was the fastest to react‚ I hypothesized that the reaction would occur the fastest with the 3% hydrogen peroxide (the highest amount of concentration) because the higher the concentration the more faster the reaction occurs and helps produce or break up the enzyme. After testing all three of my substrate concentrations with 10 trials each‚ my data showed (first graph) that the 3% substrate concentration had the fastest average
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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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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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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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Enzymes Reactions to Changes in Substrate and Inhibitors Benjamin J. Mora Coronado University of Texas Rio Grande Valley at Edinburgh Abstract Purpose for the experiments was to test the enzymes in various scenarios and see how changing this would affect the rate of reaction. The enzyme source used in the experiments was Turnip Extract. Concentrations of Turnip extract for activity 1 where o.5ml‚ 1.0ml‚ and 2.0 ml as for the rest of the activities 2 Through 4 stayed at a consistent concentration
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Abstract: Enzymes‚ molecules that speed up chemical reactions‚ are specific to one substrate. In this experiment the substrate hydrogen peroxide and the enzyme catalase will be used. The higher the concentration of potato extract‚ or catalase‚ the faster the reaction and the more substrate present will result in a decrease in the time of the reaction. The amount of concentrations of enzymes and substrates are changed to determine if the reaction is further catalyzed by a greater concentration of enzymes
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