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Horseradish Peroxidase Lab Report

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Our group discovered a novel enzymatic activity by placing horseradish peroxidase (HRP) in presence of ARGET ATRP reagents for the polymerization of N-isopropylacrylamide. 16 Reactions without one of the reagent, i.e. reducing agent, catalyst or initiator, yielded no polymers. Analysis of the polymers formed via COSY 1H NMR confirmed the presence of ATRP initiator in the polymer chains. Neutron scattering experiments revealed that 67% of end-chains were bromine terminated pointing toward an ATRP mechanism. The reaction was highly dependent on pH and optimal condition at pH 6 yielded polymeric chains with dispersity as low as 1.44 were synthesized. As none of the other reagents are affected by pH, this constituted the first evidence of the …show more content…

The reasoning is that the active center alone is not sensitive to its environment and reaction conditions as the enzyme. Therefore, using solely the active center would make it a more robust catalyst. 3. Enzyme mimetic catalyzed ATRP The first study of this type of catalyst was carried out by Simakova et al.22 They started using hemin which is like the iron surrounded by porphyrin found in HRP, hemoglobin or catalase to polymerize PEGA. However due to its low halidophilicity, low solubility in water and possible incorporation in polymer chains due to its double bonds, controlled polymerization could not be achieved. Addition of KBr to reinforce deactivation but also to fasten initiation permitted to obtain polymer with narrow dispersity. This was considerably enhanced upon PEGylation of the catalyst to increase its water-solubility. Concurrently, Yamashita et al.23 reported the polymerization of NIPAM also using hemin as catalyst. However, they obtained quite broad dispersity confirming that hemin itself does not suffice to obtain control over the reaction. However, they could show that polymer were formed via an ATRP-like

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Methods of Data Collection Measuring the independent variable: The pH (the independent variable) is being tested on the turnip peroxidase to observe the reaction rates. 5 levels of pH are required for these series of reactions so pH buffers of 3, 5, 7, 9, and 11 are to be placed in each of the waters that will be put into the cuvettes for the experiment. Measuring the dependent variable: A colorimeter must be used in order to calculate the reaction rate/absorbance level of the turnip peroxidase when the different pH levels affect it. The colorimeter can be used to measure the transfer of heat to or from an object.

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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. In this lab, the source of hydrogen peroxidase was the potato solution. The substrate that the hydrogen peroxidase acts upon is the hydrogen peroxide.

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Anthracene-9,10-bismethylmalonate (ADMA), Orange G and polystyrene (PS, Mw = 192,000 g/mol) were purchased from Sigma-Aldrich. Acetic acid (glacial), tetrahydrofuran (THF) and dimethylformamide (DMF) were purchased from Saarchem, while Rose Bengal was purchased from Fluka. Water collected from milli-Q water (Millipore corp., Bedford, MA, USA) was used for the preparation of all aqueous solutions. All solvents were dried prior to use using molecular sieves. BODIPY 1 was synthesized using the method described previously described (Fig. 1) [16].

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the help of the enzyme phosphoglucose isomerase ( PI ) this reaction occurs involving an isomerization reaction. This reaction includes the rearrangement of the the carbon-oxygen bond to transform the six membered ring. Rearrangement takes place when the six membered ring opens and then closes in such a way that the first carbon becomes now external to the

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purpose the propose of this experiment was too see if the chemical reaction of a enzyme can be made faster. Hypothesis I think that a warm environment would be best to make an enzyme’s reaction faster. because a protein can move faster in heat.

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Introduction The purpose of this experiment was to determine the presence of the peroxidase enzyme and determine its function in relation to plant cells. This enzyme is significant because peroxidase protects plant cells from invading microorganisms and toxic chemicals. In order to find the presence of this enzyme, this required the group to prepare a sample of a vegetable that would be transferred to a sheet of tissue. After transferring the plant cells to the sheet and adding a series of substances to the cells, a purple staining on the tissue would detect the presence of the peroxidase enzyme.

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In this lab we determined the effect of PH after their mixing of the substances to get the result of the peroxide strength or weakness during the experiments of Spectrophotometer by using test tubes and absorbance V’s time activities over Enzyme concentration, PH, Temperature, and inhibitors on the Peroxidase reaction. A future experiment might include an additional calibration using the new and advanced Spectrophotometer soft wear and others technologies such as the reactions of the compounds with Peroxide and other materials to further test the nature of the PH and more positively or negatively we will identify the PH effect on Enzyme. Increasing the temperature increases reaction rates because of the disproportionately large increase in

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If the enzyme becomes denatured the substrate will not be able to bind to the active cite, and if the enzyme becomes too cold the reaction will never occur

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Unlike step-growth, the monomers in chain-growth do not exist as oligomers for a long period of time, but rather combine rapidly to form polymers. If a small molecule byproduct is produced along with the final product, then the polymerization is known as a polycondensation. If no byproduct is produced, then the polymerization is known as polyaddition. In this experiment, polyamide nylon-6,6 was produced and characterized as a step-growth polycondensation that produced water as a byproduct. In order to produce Nylon-6,6, hexamethylenediamine and adipoly chloride reacted in a solution of 20% sodium hydroxide.

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protein. The experiment uses two sets of T2 bacteriophages. DNA has P but no S and Protein has S but not P. They also knew that something from T2 phage entered E. coli cells and directed the bacteria to produce more phage. They assumed that the genetic material was the material that entered the cell. So they set out to determine the chemical nature of the material.

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As shown in Figure 1, the sample containing 2 ml of the enzyme had the greatest rate of absorbance change (m= 0.007) when mixed with substrate and dye (Figure 1), indicating that the substrate was being converted to product faster than the samples that contained 0.5 ml and 1 ml of enzyme. The second experiment included the measurement of temperature effects on Catalase. The results varied for each temperature used. The optimal temperature for this enzyme was forty-eight degrees Celsius.

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This has been reported in the literature. Amount of reagents that were used for synthesizing both PCL and PCLF samples were calculated based on theoretical calculations in order to obtain that certain MW of the polymer (Appendix I and II). In this experiment, GPC was used to obtain the exact molecular weight of the polymer. As seen in Table 8, the expected MW for PCL 3000 and PCL 9000 were 3000 g/mol and 9000 g/mol respectively. However, the GPC results obtained for PCL 3000 and 9000 were 6800 g/mol and 15000 g/mol

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Today, one of the most common use of biocatalyst is in the synthesis of Januvia, a medicine which treats type II diabetes. The enzymatic process provides a more eco-friendly production while increasing the yield and eliminate the need for a metal catalyst. The original way of producing Januvia was to use rhodium to catalyze the asymmetric hydrogenation to produce the active pharmaceutical ingredient (API), sitagliptin (Taylor, 2012). This way of production required a high pressured hydrogen environment and the use of a metal catalyst.

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An important aspect of enzyme-catalyzed reactions is saturation, where at low substrate reactions, the rate of the reaction increases as the substrate concentration is increased. Eventually, there will reach a point where the enzyme is performing at the maximum activity so the reaction rate is no longer dependent on the substrate concentration

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In order for an enzyme to act on a substrate, the substrate has to enter the active site with the minimum rate of energy for the reaction to occur.

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