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 At specific instances, aliquots of the reaction mixture were withdrawn and quenched with acetone.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.
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.
Purpose: The purpose of this lab is to titrate an unknown solid acid (KH2PO4) with a standardized sodium hydroxide solution. After recording and plotting the data, the acid’s equivalence point will be recorded once the color changes. Using the equivalence point, the halfway point will be calculated, which is used to determine the acid’s equilibrium constant. The acid’s calculated equilibrium constant will be compared with the acid’s established pKa value. Eventually using the NaOH and the acid’s consumed moles, the equivalent mass will be determined.
The purpose of this experiment was to perform a Wittig reaction using two different methods: In method I, 250 mg aldehyde was mixed with 785 mg phosphonium salt in 5 M NaOH solvent. This mixture was stirred for thirty minutes and filter by vacuum filtration for the product. In method 2, 250 mg of aldehyde, 785 mg, benzyltriphenylphosphonium chloride, and 380 mg potassium phosphate tribasic were homogenize with a pestle and mortar. Vacuum filtration was also used in this method to attain the product. The products in both methods were used for recrystallization and TLC.
In the next steps the density of water between 30-40 °C, 40-50 °C and 50-60 °C was measured. Then our results ρ vs T and also density vs temperature values given in the Steam Tables were plotted on the same graph in order to compare. In the second part the density of water was measured by density bottle. The densities obtained from the experiment are 995, 992.5, 991, 990 kg/m3 for the first part and
ZPFe (3 mol%) was added to a mixture of a benzoyl chloride (10 mmoL) and an aromatic compound (10 mmoL). The reaction mixture was stirred for the appropriate reaction times at 80 °C (Table 2). After completion of the reaction (monitored by thin-layer chromatography, TLC), the mixture was diluted with Et2O and filtered. The organic layer was washed with 10% NaHCO3 solution and then dried over anhydrous Na2SO4. The solvent was evaporated under reduced pressure and the product purified by column chromatography on silica gel to give the corresponding pure aryl
The solvent system used for analysis was 10 mM NaOAc/ 150 mM NaOH and the kestoses were eluted at a flow rate of 1 mL /min. 3.2.2. Investigation of reaction parameters There are certain reaction conditions that may favour the production of one kestose isomer over the other. Therefore, several parameters (pH, temperature and time) were chosen and investigated to develop the optimum reaction conditions for each of the kestoses. The experiments for each parameter was carried out in triplicate.
C is plotted and fitted to a logarithmic-line to illustrate the saturation effect, shown in Figure 1. Then using equation 12.8 in the lab manual, C/Y is calculated and plotted versus C and fitted to a straight line, shown in Figure 2. From the fitted line, Ymax, which is the maximum number of moles of acetic acid that can be adsorbed on the surface of the charcoal per gram of charcoal, can be calculated from the slope. Then, using Ymax and the value of the y-intercept, K, which is the ratio between the rate constant k1 of the forward reaction (adsorption on the charcoal) and the rate constant k-1 (detachment from the charcoal), can be determined. For calculations, refer to Appendix E. Finally, multiplying Ymax by Avagadro’s number will give the number of AA molecules adsorbed on the surface of one gram of charcoal at saturation.
The concentration of para-nitrophenol (pNP) was then quantified, following the procedure below. The solution at 33 degrees celcius was also tested to act as a negative control sample. A standard curve for pNP concentration was generated using 3ml of 0.0, 0.1, 0.5 and 1.0 mM, recording absorbance at a wavelength of 410 nm using a spectrophotometer (SpectrovisPlus Vernier). The absorbance of experimental samples was determined in an identical manner and then converted into concentration values via the standard curve. The relative enzyme activities were calculated as μmoles pNPP/minute and analyzed via a students’ T-test (Microsoft Excel 2010, Microsoft, Redmond, WA,
UF systems commonly consist of three steps: (1) A pre-concentration step achieving similar concentrations of low molecular weight components in retentate and permeate (2) A diafiltration step to purify retentate by addition of diafiltration liquid, and (3) A final concentration step to maximize the concentration of high molecular weight solutes in retentate. Literature on purification of peroxidase from Raphanus sativus is santand requires minimum number of purification steps to minimize the cost. The current study focuses on developing a purification process for radish peroxidase from the roots of Raphanus sativus. Since plant peroxidases are present in low concentration in the extract, its recovery and purification involves traditional downstream processing steps. The grinding/extraction, precipitation/concentration and different chromatographic separation techniques are the general steps involved in purification of enzymes (Fig.