eventually falls in the liquid with a constant speed of 6.0 cm s . k www.studyguide.pk www.studyguide.pk www.studyguide. (i) For this sphere travelling at constant speed‚ calculate k www.studyguide.pk www.studyguide.pk www.studyguide. 1. its kinetic energy‚ k www.studyguide.pk www.studyguide.pk www.studyguide. k www.studyguide.pk www.studyguide.pk www.studyguide. k www.studyguide.pk www.studyguide.pk www.studyguide. k www.studyguide.pk www.studyguide.pk
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effect of pH on amylase activity Aim The aim of the experiment is to determine the effects of different pH and the rate of reaction on fungal amylase and starch. Introduction The enzyme amylase is found in the human body‚ it catalyses the hydrolosis of internal glycosidic bonds in polysaccharides‚ the breakdown of starch into sugars. Amylase is present in human saliva‚ where it initiates the chemical process of digestion. Enzymes work best at an optimum pH of 7 which is the bodies normal
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CHEM 1112 Kinetics of the Persulfate – iodide Clock Reaction The purpose of this experiment is to determine the rate law and the activation energy for the reaction between persulfate ion‚ S2O82-‚ and iodide ion‚ I-: S2O82-(aq) + 2 I-(aq) 2 SO42-(aq) + I2(aq) The rate law can be written as Reaction rate = (1) Where m and n are the orders with respect to S2O82- and I-‚ respectively‚ and k is the rate constant. Determining the rate law involves determining the values
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being digested with EcoRI restriction endonucleasse. Procedures: λ DNA and puC18 DNA were put into two tubes respectively. Then‚ EcoRI buffer‚ EcoRI enzyme and deionized water would be put into both tubes. EcoRI enzyme was the restriction enzyme that cut the DNA at the specific sequence. The EcoRI buffer enhanced the stability of many enzymes and binds contaminants that may be present in DNA preparations. DI water was used to bring the solution into a required volume for gel electrophoresis.
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The kinetic theory of gases describes a gas as a large number of small particles (atoms or molecules)‚ all of which are in constant‚ random motion. The rapidly moving particles constantly collide with each other and with the walls of the container. Kinetic theory explains macroscopic properties of gases‚ such as pressure‚ temperature‚ or volume‚ by considering their molecular composition and motion. Essentially‚ the theory posits that pressure is due not to static repulsion between molecules‚ as
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MISEP Chemistry 512 – Jacobs Enzyme Catalyst Lab - Formal Report – August 8‚ 2007 ABSTRACT This investigation examined what would happen to the rate of an enzyme-catalyzed reaction if the concentration of substrate changed. We hypothesized that if the concentration increased‚ then the reaction rate would also increase. To test our question‚ we varied a combination of substrate and buffer‚ totaling 6mL‚ with a constant amount of 2 drops of catalyst. The enzyme catalyst‚ peroxidase‚ increased
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LABORATORY REPORT Activity: Enzyme Activity Name: Angela Collins Instructor: Catherine Rice Date: 07.09.2014 Predictions Sucrase will have the greatest activity at pH 5 Sucrase will have the greatest activity at 70 °C (158 °F) Sucrase activity increases with increasing sucrose concentration Materials and Methods Effect of pH on Enzyme Activity Dependent Variable amount of product (glucose and fructose) produced Independent Variable pH Controlled Variables temperature‚ amount
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An experiment to investigate the effect of temperature on the rate of reaction of the Enzyme Trypsin. Aim: This investigation was on the effect temperature has on the rate that the enzyme trypsin hydrolyses its substrate‚ a protein found in milk (casein). This investigation was conducted under controlled conditions‚ the temperature being the changeable variable. Trypsin and its substrate (powdered milk which is a source of the protein casein) were heated in a water bath. The contents of the two
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Procedures for Part A: For Activity A‚ we first tested enzyme activity. First‚ we used an H2O2 syringe to transfer 10 mL of H2O2 into an unlabeled 60-mL cup. Then‚ we used a transfer pipet to add one mL of catalase solution into the unlabeled 60-mL cup that we put H2O2 in. After that‚ we observed the solution for one minute. Then we tested the effect of boiling on enzyme activity. First we used a transfer pipet to transfer 4 mL of catalase into a test tube. After that‚ we placed the test tube filled
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Enzyme as protein Dr.Samina Haq Quantitative and qualitative test for protein and amino acids • 1. 2. 3. 4. 5. 6. Qualitative test Ninhydrin test Biuret test Xanthoproteic test Millons test Hopkins-cole test Nitroprusside test Quantitative test 1. 2. 3. Spectrophotometric assay Protein shows maximum absorbance at 280nm due to presence of tyrosine and tryptophane. Biuret test shows 540nm Lowry test shows 750nm Ninhydrin Test • Amino acid containing a free
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