This experiment was performed in order to analyze the effects of pH‚ enzyme concentration‚ and temperature on the catalytic rate on enzyme ALP. The initial experiment was done to approximate the optimum pH for the activity of the enzyme. The hypothesis was that alkaline phosphatase activity will be critically affected by pH effects. The hypothesis was valid because the data shows that the pH values for the acidic‚ basic‚ and neutral tubes increased over time‚ absorbing at similar rates. The basic
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Effecting the Reaction Rate in Enzymes in Plants and Animals Problem- How do variables temperature and surface area affect the rate of reaction occurring in the enzyme? Information- Enzymes are proteins that act as biological catalysts. They speed up chemical reactions that take place in cells. Enzymes can be found in both liver and potato. They provide a site where reactants can be brought together to react. These reactants are called substrates that fin into the enzyme. The changing of heat‚
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Enzymes and ATP Enzymes act as protein catalysts in biochemical processes Enzymes bind to a substrate and forms the enzyme substrate complex. Enzymes work by lowering the energy of activation. Activation energy must be supplied for the reaction to begin‚ once supplied‚ the reaction can proceed on its own. Enzymes can speed up events. They are not used by during the reaction because the enzyme stays the same‚ it does not change during the reaction. (Hudon-Miller‚ Enzymes‚ 2013) Enzymes act as
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Influence of Concentration on the Activity of Amylase Title Influence of Concentration on the Activity of Amylase Abstract Does more or less concentration speed up the reaction rate of amylase in starch? In this experiment diluted solutions of amylase were created and then tested using a starch solution‚ I2KI for reaction times. The answer to the question was proved to be that more concentration of amylase speeds up the reaction time. Introduction The enzyme‚ amylase is found in
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Enzyme Lab Report Introduction The objective of this experiment was to determine if changes in pH or temperature affected the activity of enzymes‚ specifically the enzyme sucrase. Enzymes are protein molecules that act as biological catalysts to increase the speed of the reaction or to lower the activation energy of that reaction. However‚ the activity of an enzyme can be affected by physical factors such as pH and temperature because these factors alter the structure of the enzyme (Freeman‚ 2011)
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The experimental samples for the pH concentration experiment were put together by using a 10ml-graduated cylinder to obtain 4ml of each pH buffer to insert into cuvettes‚ a micropipette was then used to obtain 0.5ml of catechol and 0.5ml of the catechol oxidase. The pH buffer was made first to avoid any denaturation of the catechol oxidase. Our positive control for this experiment was pH 7 because that is the pH level of most cell membranes in the cytoplasm (Whitson‚ 2016.) Our negative controls
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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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Chemistry Unit 1 – Revision Questions Chemistry 1A 1) Define an element. How many are there in the Periodic Table? 2) Write a table with the charges and masses of protons‚ neutrons and electrons. 3) Define atomic number and mass number. 4) Draw electron (energy level) diagrams for Be‚ S‚ Al‚ Cl and K. Also‚ write down the number of protons and neutrons for each. Finally‚ write the symbols (with mass no. and atomic no.) 5) Why have all Group 7 elements (halogens) got similar chemical properties
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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 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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