What predictions would you make about the enzyme activity if you were to continue to change each of the factors in Parts A – E? The predictions that would be concluded about the enzyme activity if it were to continue and change each of the factors in Parts A – E, would be that enzyme activity will decrease due to the optimal temperature, pH, concentrations, and metal salt concentration not being obtained. How does changing the concentration of enzyme affect the rate of decomposition of H2O2?…
INTRODUCTION: The objective of this lab is to measure the activity of an enzyme and the effects of environment conditions on enzyme activity. Enzymes are catalysts; agents that speed up chemical reactions by lowering the activation energy required. This means that a catalyst helps reactions occur at a greater speed and lower temperature.…
The effect of altering temperature on the rate of liver enzyme activity is measured in this experiment to be able to visualize how temperature in the environment and in the body can manipulate the rate of enzyme activity. Enzymes are protein catalysts that lower the amount of activation energy required to start a biochemical reaction. According to Dr. Meyertholen (2015), enzymes are structured to work with certain substrates, meaning that the structure determines the function of the enzyme. If the enzymes shape is altered, they become denatured. Denaturation of an enzyme can occur with changes in factors such as temperature, pH, or salinity.…
The specificity of enzymes helps make them powerful tools in nature; they are allowed to form enzyme-substrate complexes. (Bioinfo.org.cn, 2015) Reaction rates controlled by enzyme can be measured using experimental methods where the factors such as enzyme, pH and temperature can be studied. These results can be…
From 10oC to 20oC, the average rate of reaction of the class results is higher than the raw results rate of reaction by a maximum of 0.75mL/sec. However, from 30oC to 50oC, the raw results presented a slightly higher lot of rate of reaction than the average rate of reaction from the class results. The highest rate of reaction difference was for 50oC, with a difference of 0.3mL/sec between the raw and average results. This information supports the hypothesis, yet the result for 10oC and 20oC do not support the hypothesis, as due to the information known about enzymes, the lower the temperature, the slower the rate of reaction should be, therefore the average rate of reaction does not support the…
In this part of the lab, we pour 20 mL of Hydrogen Peroxide and 1 mL of yeast catalase in the reaction chamber and then submerge it in the water bath. After it was done, it can be concluded that the gas levels increased because when we first started timing it, the gas levels were at 76, but as time went by, the gas levels started to increase and in the end of the last interval, the gas level increased all the way up to 100. This result occurred because there were many active sites that were empty for the substrate to bind to and since they binded to the active sites, it started increasing a lot at the beginning. However, when the active sites started getting more occupied, the substrate could not bind to as much active sites, so the gas levels started to increase alittle less as time went on and in the end, there was no active sites that were…
ABSTRACT: Enzymes are catalysts, speeding up of chemical reactions, of biological systems by lowering the activation energy (Transitioned from the AP Biology Lab Manual). In addition, in order to determine the rate of an enzymatic reaction, one must measure a change in the amount of at least one specific substrate or product over time. We were curious about determining the effects of pH and heat on enzymatic activity because these are factors that usually affect the shape of an enzyme. We measured enzyme activity using an indicator for product at different pHs and temperatures.…
DISCUSSION Nelson et al, 2008, state “all enzymes that exhibit a hyperbolic dependence of V0 on [S] are said to follow Michaelis-Menten kinetics”. The data gathered from this experiment and plotted in figure 6 shows that it is this pattern shown in the reaction of PNPP to PNP catalysed by acid phosphatase, where a hyperbolic curve is observed in the graph of rate of reaction against substrate concentration, approaching the Vmax asymptotically. Acid phosphatase behaved congruently to the Michaelis-Menten model. Vmax was determined as 6.65 x 10-3 µmol/min using the Lineweaver-Burk plot.…
The goal of this experiment was to determine the Michaelis constant (Km) and also the maximal velocity (Vmax) and the inhibition of alkaline phosphate. In order to accomplish these goals, 5 samples were used. Each sample contained different volumes of 0.2 m MPNPP (p-nitrophenylphosphate) and 0.2 M Tris-Hcl at a pH of 8.0. To each sample 0.2 mL of the enzyme studied (Alkaline Phosphatase) were added upon insertion on the spectrophotometer apparatus. With intervals of 20 seconds their absorbance at a wavelength of 410 nm was recorded at time frame of 2 minutes for each solution.…
We were asked, "Where does the oxygen (O2) come from?" Hydrogen peroxide (H2O2), the liver, or both? The oxygen comes from hydrogen peroxide. The substance in the liver interacts with the hydrogen peroxide. The hydrogen peroxide is altered when two substances are combined.…
Discussion: The specific purpose for this study was to see how enzyme activity would change as there was a change in temperature and pH. Both temperature and pH were hypothesized to have an affect on enzyme activity. Each had an optimal temperature. At this point, the rate of enzyme activity would stop increasing and begin to decrease. For temperature, it was hypothesized that the optimal temperature would be 48°C.…
The average absorbance rate in figure 2 presents the different levels of reaction in terms of the chemical compounds. Comparing the average values (Team 1 representing our results) there is not much of a pattern when viewing the absorbance for each specific test tube for each team. Although, there are some values that were around the same range including test tube 2. As for enzyme change, the high amount of enzymes increases the absorbance that shows an increase in reaction as seen in test tube 4 (figure 1). However, because of the decrease at 30 minutes the results take a shift.…
The purpose of conducting this experiment was to explore how different factors affect the reaction rate of enzymes reacting with their corresponding substrates in order to learn more about how enzymes function in different environments. The independent variables investigated in this experiment were the concentration of different substrates, the temperature of the environment, and the effect of a catalyst on the reaction rate. The dependent variable for all of the investigations was the time it took for the reaction to occur. To investigate the effect of the concentration of the substrate on the reaction time, four test tubes were used.…
As enzyme concentration increased, the color strength continued to increase. In Biology in the Laboratory, this is confirmed by the section concerning the effect enzyme has on activity (Helms et al,. 1998). In Figure 4, the substrate and color relation had a direct relation to an extent. As substrate concentration increased, the color strength continued to increase until the solution reached maximum velocity.…
Many factors can affect the enzyme activity (including temperature, pH, substrate concentration), so all conditions apart from the one being quantified should be standardised. The…