Pmh Model Essay

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.

40 mL of a concentrated solution of sucrose was prepared at 200mg/mL. Using appropriate dilutions of the stock, 11 solutions including a control solution were made in plastic tubes. The enzyme reaction with sucrose was run in 2 mL volume at room temperature in water. The enzyme constituted half the volume of the stock solution. The substrate was added to the enzyme in order to start the reaction. Each reaction ran for 5 min after which 2 mLs of DNS reagent was added. The solution was boiled for 10 min and the results were read using a spectrophotometer.

Enzymes react differently under different conditions and concentrations, being the most productive at the enzymes specific optimum condition and concentration. The enzyme sucrase, extracted from yeast, breaks down the complex sugar sucrose into the simple sugar glucose. Testing for sucrase’s optimum environment, multiple reactions were ran using varying amounts and concentrations of sucrose and sucrase at different pHs and temperatures. The product was then treated with Benedicts solution to visually observe what amount of glucose was present after the reaction was ran; negative results being little to no glucose present and positive results being

An Investigation on the rate of reaction of the enzyme Catalase on the substrate Hydrogen peroxide.

Effect of pH on Enzyme Activity. 1. Dependent Variable. amount of product (glucose and fructose) produced 2. Independent Variable. pH 3. Controlled Variables. temperature; amount of substrate (sucrose) present; sucrase + sucrose incubation time

The concentration of glucose in Gatorade was analyzed with a calibration curve, and to insured the best fit was used all R2 were of 0.99 or better (Figure 1). The calibration curve created with data of samples 1 to 7, with glucose concentration that ranged from 0.1mM to 0.06mM (Table 1). The calibrated samples were made with known glucose and to attain the concentration of glucose, specific enzymes that react with ferrocyanide and glucose were used. The first reaction of glucose oxidase, O2 and glucose were bind to create beta D-glucolactone and hydrogen peroxide. The hydrogen peroxide with a 1:1 stoiquiometric ration to glucose is catalyzed by horseradish peroxidase to Ferrocyanide. (lab manual) The final product of the enzymes catalysis is

They had to work in Tobacco field 6 days a week and 12 hours a day

Glucose is very important in our daily lives. It gives us energy to carry out all of our activities. Cells in our bodies need glucose to respire and in the process release the energy we need. Glucose is also a type of carbohydrate. It has a chemical formula of C6H12O6 and is a monosaccharide reducing sugar (Kolej Mara Banting – Students’ Handbook for Biology HL Year 1). It is the simplest form of carbohydrate. In this experiment, sulphuric acid, H2SO4 and potassium permanganate, KMnO4 is added into glucose with different concentration and the time taken for the purple pink colour of potassium permanganate solution to change to colourless is recorded. This is because glucose donates electrons to the permanganate

We hypothesized that a medium pH buffer added to the hydrogen peroxide an peroxidase reaction would be the best condition for the enzyme activity due to it being the more neutral than the high, being basic, and low, being acidic, pH.

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 to determine the temperature and pH effects on Peroxidase activity. Lastly, to determine the effect of an inhibitor on Peroxidase, an inhibitor is added to the extract. It was found that an increase in enzyme concentration also caused an increase in the reaction rate. The reaction rate of peroxidase increases at 40oC. Peroxidase performed the best under pH5 and declined as it became more basic. The inhibitor (Hydroxy-lamine) caused a decline in the reaction rate. The significance of this experiment is to find the optimal living conditions for Peroxidase. This enzyme is vital because it gets rid of hydrogen peroxide, which is toxic to living environments.

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

The experiments involved PH buffers of different pH were added to potato juice, water, and the enzyme catecholase. The mixture was then subjected to spectrophotometer at a wavelength of 420nm taking the absorbance readings. In the second experiment, a phosphate buffer of PH 7.0 was used in different measures together with different measurement of potato juice and the enzyme catecholase then subjected to the spectrophotometer at a wavelength of 420nm. The data collected inform of table and analyzed using descriptive statistics such as line graph and later interpreted, showing that PH and enzyme concentration do affect the rate of enzyme reaction

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

The purpose of this lab report is to investigate the effect of substrate concentration on enzyme activity as tested with the enzyme catalase and the substrate hydrogen peroxide at several concentrations to produce oxygen. It was assumed that an increase in hydrogen peroxide concentration would decrease the amount of time the paper circle with the enzyme catalase present on it, sowing an increase in enzyme activity. Therefore it can be hypothesised that there would be an effect on catalase activity from the increase in hydrogen peroxide concentration measured in time for the paper circle to ride to the top of the solution.

2cm of a solution was tested and added 2 cm of 10% of potassium hydroxide solution and the test tube was shaked.