TLC, NMR, and IR spectroscopy were used throughout the process to identify ferrocene and acetylferrocene in addition to evaluating the levels of purity. Evidence: The objective of our experiments was to prepare acetylferrocene from ferrocene. The overall reaction was carried out using 6.1 equivalents of liquid acetic anhydride to 1.8 equivalents of phosphoric acid and concluded with an aqueous workup with NaOH. The initial reaction mixture containing ferrocene, acetic anhydride, and phosphate acid was mixed on a hot stir plate. During this period, reflux was observed, and the mixture appeared dark brown in color.
In order to determine the value of X, the hydrate is heated on a burner to undergo decomposition reaction to be decomposed into CuSO4 and water vapor. Water vapor is evaporated during the reaction, leaving CuSO4 crystals, which is supposed to be white, in remain. By weighing the mass of CuSO4 and the mass difference of substance before and after the reaction, the mole of CuSO4 and H2O can be calculated. The value of X can thus be determined by calculating the mole ratio of CuSO4 and H2O. In the lab, through calculation, the value of X is determined to equal to 5.361211229, which is close to 5.
Because it is a tertiary benzylic halide, the reaction is considered an SN1 type. To test the purity, the class then uses a TLC. When one places,” a spot of the substance on the absorbent surface of the TLC plate, the solvent (or solvents) run up through the absorbent,” (Zubrick223). The initial mass of the reactant, triphenylmethyl chloride was 2.006 grams. The experiment yield is 1.589g, which is a 80.3% yield.
The purpose of this experiment is to perform a two step reductive amination using o-vanillin with p-toluidine to synthesize an imine derivative. In this experiment, 0.386 g of o-vanillin and 0.276 g of p-toluidine were mixed into an Erlenmeyer flask. The o-vanillin turned from a green powder to orange layer as it mixed with p-toludine, which was originally a white solid. Ethanol was added as a solvent for this reaction. Sodium borohydride was added in slow portion as the reducing agent, dissolving the precipitate into a yellowish lime solution.
The purpose of this experiment was to analyze the rate of the catalyzed decomposition of hydrogen peroxide in regard to the effects of concentration and temperature. 2H2O2 (l) —I-—> 2H2O (l) + O2 (g) In part one of the experiment, catalyst KI was added to varying solutions of 3% hydrogen peroxide and DI water and the composition of hydrogen peroxide was observed. This was observed by collection the volume of oxygen gas produced during the decomposition, and measuring its volume. From that, volume of oxygen gas produced was plotted against time and a linear least square fit line was generate. From the line equation, rate was derived, rate is equal to the slope of the line.
a. What are Enzymes Enzymes are very efficient protein based catalysts for biochemical reactions, which are essential to all living this to sustain life. Enzymes itself are not alive as they are proteins, however they are still made by living things and act as a catalyst to speed up the overall chemical reaction, asmost chemical reactions in biological cells would occur too slowly if it was not for these enzymes. Despite them making chemical reactions move quicker, they are not changed by the reaction. b. Optimal Enzyme Temperature There is a certain temperature at which an enzyme's catalytic activity works at its best and is at its greatest.
The values of the reaction orders determine the dependence of the reaction rate on concentration of the respective reactants and generally have a following value: 0, 1, -1, or 0.5. The Reaction Orders (“x” and “y”) will be determined experimentally by measuring the initial rate of five experiments with varying concentrations of one reactant independently of the concentration of the other reactant (B). This allows us to determine the dependence of the rate on the concentration of persulfate and the numerical value of the Reaction Order with respect to reactant persulfate. This investigation involves conducting the iodine clock reaction, a reaction between sodium persulfate and potassium iodide. During the experiment, a colourless solution of potassium iodide and a solution of sodium persulfate, starch and thiosulfate will be combined into a beaker to later react into a blue-black complex.
The effect of pH on the speed of enzyme interaction with substrate chemicals Hypothesis: About pH: If the pH level is less than 5, then the speed of the enzyme reaction will be slower. About temperature: If the temperature stays the same, then the speed of the enzyme reaction will not be completely affected. Background information: The function of enzymes is to speed up the biochemical reaction by lowering the activation energy, they do this by colliding with the substrate. All enzymes are under the class of protein biomolecule. Amino acids are the basic units that are combined to make up an enzyme.
The UV sensitive bands were purified using repetitive preparative TLC followed by crystallization. The identity of Ecdysterone was established by the following procedure: HPLC, with a Shimadzu LC-20, a Phenomenex C-18 reverse-phase Luna C18 which was used with a mobile phase of MeOH:Water (1:1) at 1.80 mL/min and the absorbance was monitored at 254 nm. Studies confirming the presence of a single peak of the isolated Ecdysterone, with a characteristic UV absorption at 246 nm were done using commercial standard Ecdysterone (Sigma) (Figure 2 A and B).
Abstract In this experiment, the reaction kinetics of the hydrolysis of t-butyl chloride, (CH3)3CCl, was studied. The experiment was to determine the rate constant of the reaction, as well as the effects of solvent composition on the rate of reaction. A 50/50 V/V isopropanol/water solvent mixture was prepared and 1cm3 of (CH3)3CCl was added. At specific instances, aliquots of the reaction mixture were withdrawn and quenched with acetone. In addition, phenolphthalein was added as an indicator.