Enzyme Catalyzed Reaction Lab

MANUAL Q5: What color of light is being absorbed by the sample solution? How is that color related to the color of the solution?

The values of color absorbance are effective because color absorbance has a linear relationship with concentration values, which in turn, allows us to easily find concentration values for many solutions. Beer’s law describes this phenomenon since the absorbance is directly proportional to concentration. We observed that as the color absorbance increased, the concentration of the FeSCN2+ complex ion increased. This is because as the FeSCN2+ concentration increases, the blood-red color becomes darker due to more presence of the blood-red FeSCN2+ ion. Therefore, the color absorbance increases because there is more blue color absorbed by the darker red color. We then graphed the absorbance and concentration values and created a line of best fit. Using the line of best fit, we were able to predict the equilibrium concentrations of the FeSCN2+ solutions and find the change required to reach equilibrium. Since we already knew the initial concentration of FeSCN2+ and since we already found the equilibrium concentration of FeSCN2+, we can calculate the change in equilibrium. Using this data, we were able to calculate the equilibrium concentration of all of the species in this lab, since we already knew the change from the initial concentration to the equilibrium change. Q is less than K because there was no initial concentration of FeSCN2+, but after the system reached

After reviewing the basics of enzymes and catalysis, we take a dive into the wonderful

Hope Spivey Gate City High School Block 4 Introduction Enzymes cause havoc and speed up reactions, but why exactly does this occur? Enzymes are biological molecules, proteins, that act as catalysts and help complex reactions occur everywhere in life.

In part II of the lab six small glass tubes were obtained in a test tube rack. Ten drops of distilled water were then added to test tube 1, five drops to tubes 2-4, and no drops in tubes 5 and 6. Five drops of 0.1M HCl were added to test tube 5 and five drops of 0.1M NaOH to test tube 6. Five drops of enzyme were then added to all tubes except tube 1. Tube 3 was then placed in the ice bucket and tube 4 was placed in the hot bucket at 80-900C for five minutes, the remaining tubes were left in the test tube rack. After the five minutes five drops of 1% starch was added to every tube and left to sit for ten minutes. After ten minutes five drops of DNSA were then added to all the tubes. All the tubes were then taken and placed in the

Objective: Measure the rate of decomposition of hydrogen peroxide with and without the addition of an enzyme catalase at different time intervals.

Through this investigation the wavelength was to be determined in which the salt solution absorbs the most light. This was necessary in order to figure the concentration needed to create a solution form scratch. Once the appropriate absorbance wavelength was chosen this granted the flexibilty to concoct a solution from scratch or form a dilution in respect to the appropriate concentration. Utilizing the Beer-Lambert Law to control the path length and the constant through this experiment using the Spec-20, allowed concentration to be used as the identifiable variable. A solution of .100 M of Nickel (2) Nitrate will be used to obtain measurements of absorbances and concentrations at varied wavelengths. These absorbances and concentrations are then used to generate a graph.

The purpose of the experiment was to change the pH of the enzymes and environment to see if there is a significant change in the enzyme’s activity. Test tubes were labeled with their designated pH containing starch ranging from 3 to 8. The amylase enzyme was then added to each test tube and the reaction occurred for ten minutes. Introducing HCL to the solution then stopped the reaction, and its absorbance was taken. The absorbance of the solution determines how active the enzyme was. If the absorbance number is high, then the enzyme was not as active because there is excess starch. When the absorbance reading is low that means the enzyme is being productive and is breaking down the starch at a relatively fast rate. The control is absorbance

H3PO4 is used to give colas a tart or tangy flavor [8]. We used three different samples, Sam’s Coke (1), Diet Coke (2) and Coca-Cola (3), in our experiment. We heated the colas without boiling the solution to remove CO2. We then used AVM (a reagent) because PO4 is colorless and when AVM reacts with PO4 it creates a yellow color that absorbs the color blue [4]. We measured each cola at 370 nm because from last week experiments the wavelength was the peak. We measured for transmittance and Sam’s Coke and Coca-Cola had the lowest. We then found the absorption using the formula, A = 2 - log10 T%. Next we used y= 23725x - 3.8814 to find the concentration of H3PO4. We used this formula because it relates the concentration with the absorbance of PO4. The results from the previous week allowed us to discover the H3PO4 in the colas. Diet coke had the highest concentration of H3PO4 because the cola had a lower absorbance, results on Table 6. The concentration of H3PO4 increases acidity of the colas.

The concentration of PNP formed increase with time, The reason behind this is because enzymes are powerful catalysts. They can accelerate the reactions by a factor of as much as a million or more. In this experiment, with the lapse of time, more substrate binds to the enzyme’s active site of which the surface is lined with amino acid residue with substitute groups that bind the substrate and catalyse its chemical transformation. Enzyme reduced the activation energy of this reaction. This enzyme-catalysed reaction takes a different 'route'. The enzyme and substrate form a reaction intermediate. Its formation has a lower activation energy than the reaction between reactants without a catalyst. Therefore more PNP formed.

They fall along the best fit-line, producing an R2 value of 0.99726. The equation that represents the relationship between absorbance and concentration is y= 0.017x + 0.1733. Next part of the experiment was to determine the absorbance of 2 unknowns at both high (100μl) and low (10μl) concentrations. The result is shown in table 2

169 nm, while the absorption coefficient at 355 nm (ag355) was used as a quantitative parameter of CDOM

Solutions can be measured in molarity, M, and molality, m, and can help experimentally find the absorbance, A, of a solution. Most solutions absorb ultraviolet (UV) or visible (Vis.) light (“Beer’s Law”). In this experiment, the dark blue color of the more concentrated solution absorbed more light than the light blue, more diluted solutions. Beer’s Law, shown in the equation A=ecl, states that as concentration increases, the absorbance of light should also increase. Out of the five known solutions, the least diluted solution, with a CuSO4 concentration of 0.50M, had the highest absorbance while the 0.10M concentration had the least absorbance.

1. At substrate concentration, the enzyme is working at “maximum efficiency.” With a concentration at 40, it produced 2,339 products.

Enzymes are known to be large protein molecules that act as a catalyst to accelerate the rate of a chemical reaction1. Specifically, enzyme-catalyzed reactions have been widely studied in the field of biochemistry for the determination of enzyme specificity and efficiency2. Determining the rate of reaction can reveal important physiological properties of the enzyme being studied. Additionally, rate expressions can provide further information that can help explain the complex nature of a specific biochemical reaction3.