Oxidation Of Cyclohexene Lab Report

There are few vegetables and fruits that turns to the color brown if their surface is exposed to oxygen. Once the veggies or fruits been exposed to oxygen, then the browning begins to appear, and electrons and hydrogen will be removed. This happens because of an enzyme called catechol oxidase. The enzyme will act on its substrate catechol to form a yellow compound which then reacts with the oxygen in the air and change into benzoquinone. The more concentration of the enzyme, the more browning appears. Catechol oxidase is found in cell cytoplasm, their function in plants are to "help protect damaged plants bacterial and fungal disease."

The purpose of this experiment was to learn about the electrophilic aromatic substitution reactions that take place on benzene, and how the presence of substituents in the ring affect the orientation of the incoming electrophile. Using acetanilide, as the starting material, glacial acetic acid, sulfuric acid, and nitric acid were mixed and stirred to produce p-nitroacetanilide. In a 125 mL Erlenmeyer flask, 3.305 g of acetanilide were allowed to mix with 5.0 mL of glacial acetic acid. This mixture was warmed in a hot plate with constantly stirring at a lukewarm temperature so as to avoid excess heating. If this happens, the mixture boils and it would be necessary to start the experiment all over again. After obtaining an homogeneous mixture, the flask was placed in an ice bath during five minutes next to a graduated cylinder containing 5.0 mL of concentrated sulfuric acid. The temperature of the ice bath was recorded to be 1.1 °C. Likewise, a second graduated cylinder containing 1.8 mL of nitric acid and 2.5 mL of sulfuric acid was immersed in the cold ice bath to keep the three different solutions at the same temperature.

One purpose of a Wittig reaction is the formation of alkenes from aldehydes or ketones

Abstract: Enzymes can catalyze chemical reactions by speeding up the chemicals activation energy. Temperature and pH are just two of the factors that affects enzymes and their involvement with chemicals and the way they function. Throughout this experiment, we conducted a study on peroxidase, which is an enzyme. The following information consist of the recordings of when it was exposed to four different pH levels to come up with an optimum pH and IRV at the end.

The acid is necessary to deprotonate the norbornene. This deprotonation removes the double bond and creates a carbonation. Water then attacks this carbocation. This is followed by a deprotonation from another water molecule to reform the acid catalyst. Then, norborneol is formed. The process of acid-catalyzed hydration of an alkene to and alcohol has valuable properties with practical uses. Naturally, as an alkene, norbornene is not very reactive. It has a strong pi bond, and is also non-polar. However, by hydrating norbornene with the assistance of an acid-catalyst, norborneol is formed. Norborneol, being an alcohol, is much more reactive and has the potential to be further reacted to obtain a certain product. These products can have pharmaceutical uses, fragrant qualities, or become other chemical compounds used in the lab. Therefore, the reaction of an alkene to an alcohol is valuable due its ability to create the reactive intermediates for useful

The purpose of this experiment was to perform a bromination reaction that converts cyclohexane to trans-1,2-dibromocyclohexane. To do this, 1 mL of 30% hydrogen peroxide was mixed with 3 mL of bromic acid in a round bottom flask containing a spin vane. The solution turned from clear to orange, dark red. The color change is a useful indicator to identified whether reaction was completed before moving to another step. Next, 1 mL of cyclohexene was pipet into this mixture, which changed the solution from red to orange and eventually yellow. The mixture was transferred into a centrifuge tube with brine solution. Two layers were formed, with a yellow layer on top and the clear bottom layer. The bottom layer is the only organic layer because it is denser. NaHSO3 was used to washed the mixture. The bottom layer was extracted by pipette and rinsed with NaSO4 for drying. The organic layer was transfer into a vial and placed under NEVEP to attain a solid product. The product was a mixture of white solids with liquid.

Cyclohexanone a cyclic ketone was oxidized to adipic acid using the oxidizing agents concentrated nitric acid. Then, the recrystallized product was characterize by using infrared spectroscopy and taking the melting points. The experiment yielded 0.199 grams of adipic acid and a very high percent yield of 106.40%. Upon examination of IR-spectrum, Adipic acid was identified by comparing it to the IR-spectrums provided in the lab book. Furthermore, the melting point of the experiment was obtained to be 151-154 ºC, which included the theoretical melting point of 153 ºC between the experimental melting point range.

Enzymes are proteins used in nearly all chemical reactions in organisms. These proteins are known as catalyst to speed up or enhance reactions. Enzymes are reliant on substrates; they are known to convert nearly one thousand substrate molecules per second during reactions (Freeman, 2017, 90). In reactions, there are other active conditions that can affect the enzyme. These include, but are not limited to different pH levels, changes in temperature, amount of inhibitor, and amount of salt.

We use peroxidase as our enzyme in the experiment. Peroxidase is found in plants, such as turnip, and can convert hydrogen peroxide to water and oxygen. We had which were hydrogen peroxide (3%) and hydroxylamine. The hydrogen peroxide competes with the hydroxylamine for the active site molecules from peroxidase. The peroxidase needs the hydrogen peroxide in order to separate it into water and oxygen. If enough of the hydroxylamine is used in the test tube, it will stop the enzyme from binding with the hydrogen peroxide causing competitive

In this experiment it was examined whether the enzyme peroxidase will work fastest in a pH of 8.0. We placed the enzyme peroxidase in a reaction with guaiacol and hydrogen peroxide in four different pH solutions. Then recorded the absorbencies for each reaction until all substrates were used up, and calculated the initial reaction velocities for each. We found that the reaction in a pH 7.0 solution had the highest initial reaction velocity. Over-all this study shows that the enzyme peroxidase will work the fastest in a 7.0 solution.

This experiment was started to measure the height equivalent of a HETP column to calculate twenty theoretical plates. The company need this information to separate the cyclohexane from the toluene. The separation was accomplished by the use of fractional distillation and gas chromatography. The process yielded one plate for the17.6cm column meaning, that the porcelain beryl saddles as a packing material are ineffective. Although the results were found to be inefficient this may have been due to an error in the calculation, or the amount of time per temperature spent collecting the fractions. These results can be improved by re-distillation of the distillate fraction.

An enzyme can not be considered a reactant because, like catalysts, the enzyme is never used up in the reaction and is reused again in another chemical reaction.

Chevron Phillips Chemical Company is the major producer of Cyclohexane. This successful company hoses the three largest cyclohexane plants in the world. Many are puzzled by how the production of cyclohexane seems to have become stagnant. Perhaps this is due to the cost of benzene increasing or the demand increasing. Through thorough investigation, the answer to this question and many more can be answered. There are two methods of obtaining cyclohexane. These two methods are fractional distillation of naphtha and hydrogenation of benzene. Research suggest that the hydrogenation of benzene is the most economical way to create our chemical of choice. According to ICIS, cyclohexane is used in the production of adipic acid used to

The peroxidase isolated from horseradish, HRP, is the most available and commonly used peroxidase. One factor that has limited its widespread and large-scale use is its high cost of production. A cost effective purification technology and exploringalternative sources with high peroxidase activity can help to bring down the cost of enzyme production. Peroxidase from roots of Raphanus sativus can serve as a cost effective alternative for HRP.

The effect of the catalyst was discovered by insertion of different molar ratios of the complex catalysts (L1VO, L2VO, L3VO and L4VO) to cyclooctene in the oxidation process (0.02, 0.05 and 0.10 : 1, respectively) using aqueous H2O2 in acetonitrile at 90 °C for 2 h (the optimized reaction conditions). In another words, the effect of the amounts of the catalysts related to the amount of the substrate (cyclooctene) on the epoxidation processes with 0.02 : 1, 0.05 : 1 and 0.10 : 1 (cyclooctene : catalyst). The results are reported in Table 9. The catalytic potentials of L1VO, L2VO, L3VO and L4VO at catalytic amount of 0.02 mmol has been studied and reported in Tables 4-7. The increase of the catalyst molar ratio to 0.05 and 0.10 mmol caused improvement in the rate of 1,2-cyclooctene oxidation with higher conversion compared to the catalytic amount 0.02 mmol of the VO-complexes. Unfortunately, the chemoselectivity was reduced by increasing the amount of the catalyst VO-complexes to be 65,