Factors Affecting the Rate of Catalase Activity

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 Effects of Varied Temperatures, pH Values, Enzyme Concentrations, and Substrate Concentrations on the Enzymatic Activity of Catecholase

Students will be observing normal catalase reaction, the effect of temperature on enzyme activity, and the effect of pH on enzyme activity in this experiment. The enzymes will all around perform better when exposed in room temperature than when it is exposed to hot and cold temperatures. This is based on the fact that the higher the temperature, the better the enzymes will perform, but as the temperature reaches a certain high degree, the enzymes will start to denature, or lose their function.

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

Lab six requires students to observe the effects of pH and enzyme concentration on catecholase activity. Enzymes are organic catalysts that can affect the rate of a chemical reaction depending on the pH level and the concentration of the enzyme. As pH comes closer to a neutral pH the enzyme is at its greatest effectiveness. Also at the absorbance of a slope of 0.0122 the enzyme is affected greatly. The pH effect on enzymes can be tested by trying each pH level with a pH buffer of the same pH as labeled as the test tube and 1mL of potato juice, water, and catechol. This is all mixed together and put in the spectrophotometer to test how much is being absorbed at 420nm. As the effect on enzyme concentration can be tested almost the same way. This part of the exercise uses different amounts of pH 7-phosphate buffer and potato juice, and 1mL of catechol mixed together in a test tube. Each substance is put in the spectrophotometer at a wavelength set tot 420nm. The results are put down for every minute up to six minutes to see how enzyme concentration affects reaction rate. The results show that the pH 8 (0.494) affects the enzyme more than a pH of 4 (0.249), 6 (0.371), 7 (0.456), and 10 (0.126). Also the absorbance is greatest at a slope of 0.0122 with test tube C that has more effect on the reaction rate, than test tube A, B, and D.

lab bench. Place a beaker from the drawer on the stir plate. Drag the bottle of NH3 to the 5 mL graduated cylinder (the smallest one) by the sink and fill the cylinder by dropping the bottle on the cylinder. Now drag the 5 mL graduated cylinder to the beaker on the stir plate and add the 5 mL of

Fill a test tube about 1/3 full with cold tap water for use in step 34.

The first experiment begun by filling a 600-ml beaker, almost to the top, with water. Next, a 10-ml graduated cylinder was filled to the top with water. Once water was added to the beaker and graduated cylinder, a thumb was placed over the top of the graduated cylinder. This would ensure that no water was let out and no bubbles were let into the graduated cylinder. Next, it was turned upside down and fully submerged into the beaker. Then, a U-shaped glass tube was attained. The short end of the glass tube was placed into the beaker with the tip inside of the graduated cylinder. Next, a 50-ml Erlenmeyer flask was received. After, 10-ml of substrate concentration and 10-ml of catalase/buffer solution were placed into the flask. A rubber stopper was then placed on the opening of the flask. After adding these, the flask was held at the neck and spun softly

The independent variable in this investigation is pH. Each individual enzyme has it’s own pH characteristic. This is because the hydrogen and ionic bonds between –NH2 and –COOH groups of the polypeptides that make up the enzyme, fix the exact arrangement of the active site of an enzyme. It is crucial to be aware of how even small changes in the

The purpose of this investigation is to discover the effect of pH on the activity of catalase, an enzyme which plays the integral role of converting hydrogen peroxide into water and oxygen, and discover which pH level it will work at the most efficient rate (the optimum). The original hypothesis states that that the optimum would be at a pH is 7, due to the liver, where catalase usually resides, being neutral. The experiment consists of introducing the catalase to hydrogen peroxide, after exposure to certain solutions; hydrogen peroxide, water and hydrochloric acids, all containing the adjusted pH, and measuring the height of froth formed, an observable representation of the activity of the enzyme. The final data indicated that

4.Measure 35mL of warm water and add them into each of the 4 test tubes at about roughly the same time. It is essential that the water is warm. Do not seal the test tube.

1 ml of water should be added to the first test tube and make a note. In the second test tube, 1 ml of methyl alcohol should be added. In the third test tube, 1 ml of hexane must be added. Lastly, the fourth test tube will be a control.

Submerge the graduated cylinder in the plastic tub so that it is completely filled with water. Hold the open end of the graduated cylinder and move it vertically upside-down where the open end of the graduated cylinder is still submerged in the plastic tub. Clamp the graduated cylinder the ring stand of the lab table to keep it in place. perforate a hole in the top of the rubber cork for the solution container. Cut a straw the length of about four inches. place the straw inside of the rubber cork hole. Set up your timer for two minutes.

5. Wet the paper with distilled water to hold it in place in the funnel. Transfer all the solution and the precipitate from the beaker using a rubber policeman. Wash the precipitate with two or three 5-mL portions of distilled water. Do this by adding each portion to the beaker in which you did the precipitation to transfer any remaining

Step 1 and 2 was repeated by using distilled water by replacing the test solution.