Turnip Lab Report

In this experiment, the naturally occurring peroxidase is extracted from homogenized turnip (Brassica rapa) pulp (Coleman 2016). Its role in the environment is to remove toxic hydrogen peroxide during metabolic processes where oxygen is used (Coleman 2016). The goal of this experiment is to evaluate the change of absorbency of turnip peroxidase within a metabolic reaction utilizing oxygen. Any change noted is indicative of the peroxidase removing hydrogen peroxide. Within this experiment, the extract will be prepared, the amount of enzyme will be standardized, and the effect of changing the optimal conditions will be observed. If the enzyme concentration is increased then the rate of the reaction decrease. If the pH of solutions used is increased

The data in proves that our hypothesis was correct. When we increased the temperature to 35°C, the the enzyme activity increased because kinetic energy increased, increasing the collisions between the substrate and the enzyme, and thus creating a higher chance of reaction. When we increased the temperature to 45°C, the enzyme activity decreased as the enzyme became denatured,because the atoms in the enzyme had enough energy to overcome the hydrogen bonds between the R groups that give the enzyme its shape From our data, we could conclude that the optimal temperature of turnip peroxidase is around 35°C and around 45°C, it will start to denature.

This lab was performed in order to discover the activity of the enzyme catecholase in different pH levels as well as its absorbance in differently concentrated solutions. A spetrophotometer was used to measure the absorbance of the enzyme catecholase in different pH solutions as well as to measure the absorbance of catecholase in solutions with different concentrations of potato juice and phosphate buffers. Absorbance of the enzyme catecholase was at an optimum level when pH was close to neutral. When pH was acidic or basic, the catecholase was less effective. Also, when there was a higher concentration of potato juice and a lower concentration of phosphate buffer, absorbance of the enzyme increased.

The purpose of this report is to find out the effect of change in the Temperature, PH, boiling, concentration in peroxidase activity. Peroxidase is an enzyme that converts toxic hydrogen peroxide (H2O2) into water and another harmless compound. In this experiment we use, turnips and horseradish roots which are rich in the peroxidase to study the activity of this enzyme. The activity of peroxidase with change in temperature was highest at 320 Celsius and lowest at 40C. The activity of peroxidase was highest at a pH of 7, while it was lowest at pH of 9.Peroxidase activity was very low and constant with boiled extract, while the activity was moderate

These results shown from this experiment led us to conclude that enzymes work best at certain pH rates. For this particular enzyme, pH 7 worked best. When compared to high levels of pH, the lower levels worked better. The wrong level of pH can denature enzymes; therefore finding the right level is essential. The independent variable was the amount of pH, and the dependent being the rate of oxygen. The results are reliable as they are reinforced by the fact that enzymes typically work best at neutral pH

In this section thermal stability of the purified enzyme was studied at pH 5.5 and all optimum conditions of enzyme and substrate concentration. The enzyme solution was preheated at different temperature 40°C, 50°C, 60°Cand 70°C for various time periods from 10 to 60 minutes. After each heat period, the enzyme was rapidly cooled in an ice bath. The activity of pectinase was determined by adding the substrate and carrying out the enzymatic reaction under optimum reaction conditions.

This experiment looked at how substrate concentration can affect enzyme activity. In this case the substrate was hydrogen peroxide and the enzyme was catalase. Pieces of meat providing the catalase were added to increasing concentrations of hydrogen peroxide in order to measure the effect of hydrogen peroxide concentrations on the enzyme’s activity. The variable measured was oxygen produced, as water would be too difficult to measure with basic equipment.

The role of an enzyme is to catalyse reactions within a cell. The enzyme present in a potato (Solanum Tuberosum) is catechol oxidase. In this experiment, the enzyme activity was tested under different temperature and pH conditions. The objective of this experiment was to determine the ideal conditions under which catechol oxidase catalyses reactions. In order to do this, catechol was catalyzed by catechol oxidase into benzoquinone at diverse temperatures and pH values. The enzyme was exposed to its new environment for 5 minutes before the absorbance of the catechol oxidase was measured at 420 nm using a spectrophotometer. The use of a spectrophotometer was crucial for the collection of data in this experiment. When exposed to hot and cold temperatures, some enzymes were found to denature causing the activity to decrease. Similarly, when the pH was too high or low, then the catechol oxidase enzyme experienced a significant decrease in activity. It can be concluded after completing this experiment that the optimal pH for catechol oxidase is 7 and that the prime temperature is 20º C. Due to the fact that the catechol oxidase was only tested under several different temperatures and pH values, it is always possible to get a more precise result by decreasing the increments between the test values. However, our experiment was able to produce accurate results as to the

In the exercise # 2 we observed the effect of substrate concentration, enzyme concentration, pH and temperature on enzyme activity. All the data showed that once potato extract was added to catechol and water the reaction varied dependent on the level of catechol. As in

Discussion: The purpose of this experiment was to observe what the normal enzyme1 (proteins that catalyze chemical reactions) activity of beef liver catalase was, and to measure the effects of extreme changes in temperature and pH on the beef liver catalase function. We also observed what the bromelain1 (proteins in pineapple) activity was in a fresh pineapple compared to canned pineapple. Enzymes are present in all living things.1 These specialized proteins speed up chemical reactions fast enough to sustain life.1 This lab was driven by the question; if there is an extreme change in temperature or pH on an enzyme catalase, or a bromelain enzyme, then that catalase or bromelain will be affected or denatured.

The Enzyme Properties Lab was performed to analyze the effects of pH, enzyme concentration, and temperature on the catalytic rate of enzymes. Many functions within the human body require/involve enzymes. It was found that enzymes have an optimal pH level, catalytic rate increases as the concentration of the enzyme increases, and an optimal temperature. The enzyme that was used throughout the experiment was ALP (alkaline phosphatase enzyme). ALP functions best at a neutral pH level, as it had the largest calculated enzyme activity of 2.05E-03. When pH went above or below the neutral value the enzyme activity tended to fall. ALP’s calculated enzyme activity tended to increase with an increase in enzyme concentration, as the calculated enzyme activity of the high enzyme concentration environment was 0.004607, which was larger than the other conditions. The last part of the experiment involved temperature and it was found that the optimal temperature for the enzyme was 32°C with a calculated enzyme activity of 0.000353. When temperature was below or above the optimal temperature the calculated enzyme activity dropped. Enzymes can begin to change shape and lose function when conditions are not appropriate, which was seen in the enzyme activity of ALP in varying environments. It can be concluded that enzymes play a major role in many reactions, but if conditions (pH, enzyme concentration, and temperature) are not appropriate enzyme activity tends to drop. The results supported the

Enzymes are high molecular weight molecules and are proteins in nature. Enzymes work as catalysts in biochemical reactions in living organisms. Enzyme Catecholase is found on in plants, animals as well as fungi and is responsible for the darkening of different fruits. In most cases enzymatic activities are influenced by a number of factors, among them is temperature, PH, enzyme concentration as well as substrate concentration (Silverthorn, 2004). In this experiment enzyme catecholase was used to investigate the effects of PH and enzyme concentration on it rate of reaction. A pH buffer was used to control the PH, potato juice was used as the substrate and water was used as a solvent.

The purpose of this experiment was to record catalase enzyme activity with different temperatures and substrate concentrations. It was hypothesized that, until all active sites were bound, as the substrate concentration increased, the reaction rate would increase. The first experiment consisted of five different substrate concentrations, 0.8%, 0.4%, 0.2%, 0.1%, and 0% H2O2. The second experiment was completed using 0.8% substrate concentration and four different temperatures of enzymes ranging from cold to boiled. It was hypothesized that as the temperature increased, the reaction rate would increase. This would occur until the enzyme was denatured. The results from the two experiments show that the more substrate concentration,

To find the effect of temperature on the activity of an enzyme, the experiment deals with the steps as follows. First, 3 mL if pH 7 phosphate buffer was used to fill three different test tubes that were labeled 10, 24, and 50. These three test tubes were set in three different temperature settings. The first test tube was placed in an ice-water bath for ten minutes until it reached a temperature of 2° C or less. The second tube’s temperature setting was at room temperature until a temperature of 21°C was reached. The third tube was placed in a beaker of warm-water until the contents of the beaker reached a temperature setting of 60° C. There were four more test tubes that were included in the procedure. Two of the test tubes contained potato juice were one was put in ice and the other was placed in warm-water. The other two test tubes contained catechol. One test tube was put in ice and the other in warm water. After

In this lab or experiment, the aim was to determine the following factors of enzymes: (1) the effects of enzymes concentration the catalytic rate or the rate of the reaction, (2) the effects of pH on a particular enzyme, an enzyme known and referred throughout this experiment as ALP (alkaline phosphate enzyme) and lastly (3) the effects of various temperatures on the reaction or catalytic rate. Throughout the experiment 8 separate cuvettes and tubes are mixed with various solutions (labeled as tables 1,3 & 4 in the apparatus/materials sections of the lab) and tested for the effects of the factors mentioned above (concentration, pH and temperature). The tubes labeled 1-4 are tested for pH with pH paper and by spectrophotometer, cuvettes 1a-4a was tested for concentration and cuvettes labeled 1b-4b was tested for temperature in four different atmospheric conditions (4ºC, 23ºC, 32ºC and 60ºC) to see how the enzyme solution was affected by the various conditions. After carrying out the procedures the results showed that the experiment followed the theory for the most part, which is that all the factors work best at its optimum level. So, the optimum pH that the enzymes reacted at was a pH of 7 (neutral), the optimum temperature that the reactions occurs with the enzymes is a temperature of 4ºC or