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.…
Nine tests tubes were used for the effects of temperature and effects of pH on the enzyme activity. Mixing two tubes at a time at four different temperatures and recording the absorbance given in twenty-second intervals found the effects that temperature and pH has on peroxidase. Tubes 2 and 3 were tested at 4°C, tubes 4 and 5 were tested at 23°C, tubes 6 and 7 were tested at 32°C and tubes 8 and 9…
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…
The first piece of liver tested was we submerged it in boiling water for roughly five minutes, we got a zero reaction rate after testing it because the extreme heat totally changes the structure of the enzyme no longer having the catalase enzyme but something different. We also submerged a piece of liver in a beaker of ice and was submerged for roughly 5 minutes we then tested it and got a reaction rate of about 1 and a small amount of bubbles created because the low temperature slowed down the speed the reaction could happen. The last test for this part was we had liver in just warm water and then tested it and we had a reaction of about a 5 and a ton of bubble almost overflowing the test tube it's because the enzymes weren’t exposed to heat that could change them but heat that would speed the reaction. The last part of our lab part D was what does pH affect the catalase activity. Our first test tube had a basic solution with a pH of 10 and the reaction rate was about a 4.…
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.…
EXPERIMENT: The effect of an acidic fluid on the activity of an enzyme INTRODUCTION: There are several factors that may influence the activity of an enzyme to include temperature and the pH levels. In order to better understand how the pH level affects the actions of an enzyme, the experiment will introduce different foods with acids and bases through mixture of direct contact. OBJECTIVE:…
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.…
The five drops of hydrogen peroxide and, when applicable, one millimeter of catalase was added to the tube first. We then executed the transformations listed above as independent variables to alter the pH or the temperature, whether it was using an ice bath or adding a base or acid solution. After two minutes had passed, we took a ruler to measure the height of the bubbles and recorded it. To analyze this new data, we compared the different amounts for each trial to deduce how environmental factors affected enzyme activity. This study is a controlled experiment designed to investigate enzymes and practice interpreting…
Part B: Change the amount of enzyme Table 4: The absorbances of 5 cuvettes that measured at 475nm during a given time interval using spectrophotometer. Time (s) Absorbance @ 475nm Cuvette 1 Cuvette 2 Cuvette 3 Cuvette 4 Cuvette 5 0 0.003 0.003 0.004 0.002 0.009 30 0.003…
In this experiment, a SDS-PAGE gel was used to analyze the protein samples from the MBP-AP and WT-AP experiments. The samples are then referenced to the ladder to determine the molecular weight of the MBP-AP and WT-AP proteins. Then the UV absorbance of the two proteins from 240 nm to 340 nm is determined using a nanovolume cuvette. The absorbance at 280 nm was then used in conjunction with data from previous experiments to determine the concentration of the MBP-AP and WT-AP protein samples. Results of experiments showed that the SDS-PAGE gel yielded expect bands and the approximate molecular weight of wild type alkaline phosphatase and maltose binding protein-alkaline phosphatase is 49 kDa and 95 kDa, respectively.…
Through this experiment we measured how fast a chemical reaction occurs, by changing the degradation rate in Albumin when added to different enzymes. Albumin is a protein found in egg white, which is considered to have important storage and nutritional functions. Albumin has also been used in medicine to treat heavy metal intoxication. We ran Albumin through four different conditions to see which would make the Albumin degrade faster. We predicted that the Albumin would degrade with pepsin the fastest since it is essential for digestion of substances in the stomach.…
Discussion In this study, the Catechol enzyme was studied under the conditions of varying pH, temperature, substrate concentration, and enzyme concentration. In Figure 1, the data suggested that the trend was neither directly nor inversely proportional, but the highest activity rate was at 24°C. Most enzymes denatured at higher temperatures of approximately 40°C, which led to the inability to see any color change (Helms et al., 1998). At lower temperatures, the enzyme was somewhat efficient because molecules move slower at lower temperatures, so enzymes lost productivity.…
The enzyme reached a maximum at its greatest absorbance point of 0.526 at 10°C, the lowest temperature tested. Enzymes are most active at their ideal temperature, allowing us to confirm that 10°C is the optimal temperature for catechol oxidase. Temperatures that are too high or too low can denature enzyme shape and function. A test was conducted, monitoring a phosphate buffer at several levels of pH. As seen in Figure 2, the phosphate buffer with a neutral pH of 7, had the highest average absorbance level of 0.513. Thus, catechol oxidase has an optimal pH of…
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…
The results support the first part of the hypothesis. The enzyme sample that was put into the hot water bath (80 ºC) had the smallest change in the rate meaning that there is no new products produced by the tyrosinase enzyme. No change in color presents that the substrates were not changed into the melanin product during the duration of 8 minute. The hot water bath was successful in denaturing the enzyme as represented by figure 1. The ice bucket samples (2 ºC) had the most change in the average absorbance over time presenting that tyrosinase enzyme was active in the reaction and could produce products from the substrates.…