Oxidative Enzymes For Lignin Removal

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 type of peroxidase is used is called turnip peroxidase. Turnip peroxidase is made up of Guaiacol and hydrogen peroxide. The reactants to the product are turnip peroxidase or called tertraguaiacol and water. The color of the react is brown. In the experiment was conducted there were baseline experiment, temperature, pH, 10X substrate, Inhibitor, and half the amount of enzyme.

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

Lactic acid fermentation: Plant and fungal cells produce alcohol as a result of fermentation and animal cells produce lactic acid

Members of two groups had designed their experiment on the effect of temperature on catechol oxidase reactions. The graph that was interpreted for this discussion is as above (Figure 6). The independent variable for this experiment was temperature, and the dependent variable was the absorbance of benzoquinone. The first data set in Figure 6 showed that an increase in temperature resulted in a gradually higher absorbance of benzoquinone until the temperature reached 55° C in which the absorbance dramatically dropped. As the temperature went from cold ice to room temperature 55° C, the absorbance of benzoquinone also increased from 0.07 Au to 0.22 Au. This was due to the fact that higher temperature can increase the kinetic energy of particles (Reece et al., 2011). In this case, the temperature was initially cold, and the catechol substrate molecules and enzyme molecules were moving in a slow motion. These particles would collide less frequently; as a result, less absorbance of benzoquinone displayed. When the temperature increased to a room

The research and observations of this lab primarily focused on the enzyme activity of the enzyme Peroxidase. Peroxidase is a large protein and is composed of more than three hundred amino acids. The enzyme was selected as it is easy to experiment with and effectively showcases the effects of varying independent variables, such as pH and temperature. Peroxidase catalyzes the decomposition reaction of the chemical Hydrogen Peroxide ( H2 O2 ) into water and an electron donating molecule, which stands for R in the written chemical equation. ( The equation is displayed below:

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

Introduction: Enzymes are proteins that are used to catalyze a chemical reaction by reducing the activation energy necessary for the reaction to take place. Enzymes are highly specific to a particular substrate and function best at optimal pH ranges and temperatures (Bursal, 2013). Peroxidase is an enzyme which can be found in many plants and animals, such as horseradish and humans. The main function of peroxidase is to breakdown hydrogen peroxide (H2O2) into water (H2O) and oxygen (O2) (Groves and Boaz, 2014). A catalytic process is used by peroxidase to breakdown H2O2 which can be harmful to an organism (Zazza et al., 2009). The purpose of this experiment was to test the functionality and efficiency of peroxidase at various pH values to determine the optimal pH of the enzyme. The hypothesis was that peroxidase would perform optimally at a slightly basic pH and

The mixture at 60 °C had values of zero for both the at temperature mixtures and the recovered mixture, indicating that the high heat completely denatured the enzyme. This leads to the conclusion that peroxidase has an optimal temperature near 22°C and anything lower will have low yield, while anything higher will denature. This proves the importance of temperature on enzyme shape and thus

During laboratory week seven of Biology 232, the experiment of peroxidase characterization in monocot plants and dicot plants was presented to the students. The plants students could choose from were radishes, turnips, and beets. The stressing of the plants was to be carried out over two weeks, during the students’ fall break, as the experimental procedures were to be carried out over laboratory weeks eight and nine to identify peroxidase activity. The two taxonomic classifications of plants are Dicotyledonae and Monocotoledonae, which were discovered in 1682 by John Ray.

ability to survive in 0°C. They also produce enzymes that stabilize lipases and proteases in heat conditions. P. fluorescens is widely used to treat plants with is for its effectiveness against other microbes. They contain enzymes that are responsible for the tolerance of oxidative stress when around plants. These microbes can convert superoxide to hydrogen peroxide and catalases the peroxide to water.

After the conclusion of our experiment we refuted our original hypothesis of, “If the type of fungus (parasite or saprophyte) affects the enzyme activity, and you measure enzymes in lion’s mane an enoki, then the lions mane will have less enzyme activity? ” because we found the opposite was apparent in our experiment. While we though the Lion's mane mushroom (parasite) would have less enzyme activity than that of the Enoki mushroom (saprophyte) because the Lion's mane mushroom grows on a living hardwood tree, while the Enoki grows on a dead hardwood tree. That we saw was that The Lion's mane (parasite) which grows on a living hardwood tree, had more enzyme activity than the Enoki (saprophyte) which grows on a dead hardwood tree.

The most frequently used heme peroxidase in the enzymatic oligomerization/polymerization of arylamines is isolated from the roots of horseradish (Armoracia rusticana) and belongs to the class III family of secretory plant peroxidases (Veitch, 2004). Similarly to all other heme peroxidases, horseradish peroxidase (HRP) has an iron(III) protoporphyrin IX prosthetic group located at the active site (Veitch, 2004), Fig. 1. The most abundant isoenzyme of HRP is HRP C (Veitch, 2004), Fig. 2. For HRP C the catalytic mechanism for the oxidation of arylamines (ArNH2) at the expense of hydrogen peroxide (H2O2) is the same, the so-called “peroxidase cycle” (Veitch, 2004), Fig. 3. Following the two-electron oxidation of the native Fe(III) enzyme in the

Candida rugosa (L1754, EC.3.1.1.3, type VII, hydrolytic activity 3377,46 U/g, protein content 16% w/w) was purchased from Sigma. This enzyme was selected for immobilization due to its nonspecific mode of action for all three positions of the triglyceride molecules (Benjamin & Pandey 1998).

In the lab, the oxidation is from a primary alcohol into an aldehyde. Specifically, 4-nitrobenzyl alcohol is being oxidized and Pyridinium chlorochromate (PCC)