Peroxidase

The Enzyme Peroxidase Case Study Lab Report Autumn Vick I. ABSTRACT: The purpose of this experiment is to learn the effects of a certain enzyme (Peroxidase) concentration, to figure out the temperature and pH effects on Peroxidase activity and the effect of an inhibitor. The procedure includes using pH5, H202, Enzyme Extract, and Guaiacol and calibrating a spectrophotometer to determine the effect of enzyme concentration. As the experiment continues, the same reagents are used with the spectrophotometer

EXPERIMENT 8D Like CAT and APX, POD (Guaiacol peroxidase) activity was higher in mycorrhizal than in non-mycorrhizal plants under deficient phosphorus condition. A marked increase in guaiacol peroxidase activity in roots and leaves was associated with increased phosphorus concentrations, POD activity in mycorrhizal Zea mays leaves was significantly decreased by about 1.1_ and 1.4_ fold at 15 and 30 mg P kg-1 soil, respectively as compared to the control. The same trend was observed for mycorrhizal

RESULTS AND DISCUSSION The ability of Pleurotus citrinopleatus and Aspergillus niger exposed to two doses of gamma irradiation (1 and 2 KGy) and immobilized on wheat straw to decolorize the dyes had been studied. Table 2 shows peaks of wavelengths of different types of dyes before and after decolorization. Peaks of reactive red 6 BX, direct brown BN, direct yellow 5 G, disperse orange 2RLS, disperse violet 3RS, sulpher black Br and sulpher brown SG were at 295, 240, 400, 444, 499, 220 and 250nm were

EXPERIMENT 8 Effect of five phosphorus levels (0, 15, 30, 60, and 120 mg P kg-1 soil) on the activity of antioxidative enzymes; superoxide dismutase (SOD), catalase (CAT), Guaiacol peroxidase (POD), ascorbate peroxidase (APX) and glutathione reductase (GR) on Zea mays plant grown for 45 days in calcareous soils with mycorrhizal (+M) and non- mycorrhizal (-M) treatments. Figure 8 shows the antioxidant (SOD, CAT, APX, POD and GR) activities in mycorrhizal (M) and non-mycorrhizal (NM) plants at different

of the enzyme peroxidase? Kranz, J. BSC 110L-H009: 12 October 2016 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

effects of pH has on a reaction rate. The reaction studied was the breakdown of hydrogen peroxide catalyzed by enzyme peroxidase. Peroxidase is a large protein containing heme co factors in its active site. Four trials were ran at pH levels of 3, 5, 7, and 9. I hypothesized that the reaction would run very quickly at a pH 7, since that is the normal condition of cells where peroxidase is found. I also hypothesized that the reaction would be slower at pH levels 3, 5, and 9. The graph shows that he

of products such as food taste enhancer or spices to pharmaceutical products. Horseradish peroxidase is an important heme-containing enzyme that has been studied for more than a century but the first ever recorded observation of a reaction catalysed HRP is found in a note published by Louis Antoine Planche (Veitch, Nigel C 2004). HRP was first detected by Theorell in horseradish roots.Horseradish peroxidase has been known to degrade certain recalcitrant organic compounds such as phenol and substituted

enzymes have an optimum pH at which they function. Enzymes can lose all activity or we can say that the rate of activity decreases for enzymes at extreme pH values. Each enzyme functions best at a different pH. As researched, the optimum pH for peroxidase is between 6.0 and 6.5, or even ranging from 6.0 –7.0 is better. The majority of enzymes have their best activity between a pH of 6 to 8. The vast majority of enzymes are proteins. Because enzymes are proteins, they are made of amino acids causing

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

in reactions by reducing the amount of activation energy required. In this lab, the enzyme peroxidase is being investigated. Peroxidase is found in a wide variety of living organisms from plants and humans to bacteria. The enzyme peroxidase breaks down hydrogen peroxide, one of the toxins that is produced. The peroxidase reaction is: 2 H2O2 → 2 H2O + O2. This chemical reaction takes the toxins in peroxidase and turns it into water and oxygen. There are three factors that affect enzyme activity. These