Experimenting With Enzymes Exploration Lab

The hypothesis is that catalase activity will increase exponentially with higher concentrations of hydrogen peroxide until all catalase active sites are filled, in which case the

The independent variable of this experiment are the environmental factors that you are testing on the rate of transpiration, so our independent variables would be bright light, fan, dark, and misted. The dependent variable is the rate of transportation because this depends on whatever environmental factor the plant is placed. The constants were things like the type of plant we used, the room temperature, the type of scale we used and how far the fan/light was placed from the plant.

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

If the substrate concentration is increased then the rate of a catalase reaction will also increase until it reaches the optimal concentration or saturation point and will remain constant. This is because there will be more substrate molecules in a higher concentration therefore a higher frequency of collisions. This increases enzyme activity and more product will be formed. However at a certain concentration the enzymes will become saturated (all

The volume of chemicals (in mL) is the controlled variable of the experiment. As it will be the same in each trial and will not be changed, it is considered the controlled variable. Another controlled variable is the equipment that is used. For each trial the same equipment is always used, and therefore is also a controlled variable. The type of chemicals themselves are also controlled as for each trial they are the only chemicals used.

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,

Enzymes are catalytic proteins, meaning they speed up – but do not create – chemical

An Enzyme is a protein, which is capable of starting a chemical reaction, which involves the formation or breakage of chemical bonds. A substrate is the surface or material on or from which an organism lives, grows, or obtains its nourishment. In this case it is hydrogen peroxide. This lab report will be explaining the experiment held to understand the effects of the changes in the amount of substrate on the enzyme’s reaction.

Five different temperatures of enzyme (spinach extract) (5°C, 20°C, 35°C, 45°C and 65°C) were added to individual measuring cylinders -each filled with 7ml of Hydrogen Peroxide (H202). The height of foam (oxygen + water) produced by the reaction was recorded for each temperature of the catalase after 30 seconds, to find at which degrees the enzyme activity had the fastest reaction rate. The data collected from this experiment suggested that the enzyme extract had the greatest efficiency at 20 °C, and the temperatures greater displayed a decline in rate of reaction.

A constant/controlled variable is the yeast that is used. This would affect the results because different yeasts could affect the rate of fermentation. This will be controlled by using the same bottle of yeast for all tests.

BACKGROUND: Catalase (the enzyme) is found in yeast, it breaks down hydrogen peroxide (the substrate) into water and oxygen according to this equation. 2H2O2(aq) -------------------> 2H2O(l) + O2(g) + catalase(aq) One molecule of catalase can break 40 million molecules of hydrogen peroxide each second. Factors that affect the rate of reaction § Increasing the temperature increases the kinetic energy at which the enzyme and substrate collide.

Enzyme catalysis is the increase in the rate of a chemical reaction by the active site of a protein. A catalyst is a substance that can help the reactants in a chemical reaction react with each other faster. The catalyst for this experiment is yeast. In this lab, the chemical combination of hydrogen peroxide and yeast are used to form a reaction of creating oxygen. The active sites of the yeast combines with the hydrogen peroxide and causes oxygen to form at various levels. Yeast is a one-celled organism belonging to the group of organisms called fungi. Yeast is sometimes used in genetic engineering to produce large quantities of enzymes that can be used for medical purposes as healing wounds and reducing inflammation (How Stuff

To anaerobically break down glucose into ethanol and carbon dioxide, yeast will use the zymase enzyme which catalyses the catabolic fermentation reaction according to the induced fit model. The zymase enzyme will form weak bonds with it’s specific complementary substrate (a glucose molecule), inducing a conformational change in the shape of the enzyme and substrate. In a catabolic reaction this stresses the substrate bonds of the substrate so that they break easily, allowing the substrate to seperate into desired products; in this case ethanol and carbon dioxide. After the zymase enzyme has facilitated the reaction the weak enzyme-substrate bonds break and the enzyme can be reused. This model of enzyme substrate binding reduces the activation energy required in the reaction, allowing fermentation to occur quicker and more readily.

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.

Hydrogen peroxide is a toxic byproduct of cellular functions. To maintain hydrogen peroxide levels the catalase enzyme deconstructs hydrogen peroxide and reconstructs the reactants into oxygen gas and water. The catalase enzyme is found inside cells of most plants and animals. Regulating the levels of hydrogen peroxide is crucial in homeostasis and analyzing it’s optimal conditions for performance is just as important. To understand the optimal environment for this enzyme, they are put into different environments based off protein activity (enzymes are proteins). Catalase samples will be put into different hydrogen peroxide environments based off pH and temperature. The more active the enzyme, the more oxygen and water it will produce. Enzyme activity can be seen through the release of oxygen in the hydrogen peroxide. Since oxygen cannot be accurately measured, the data will consist of the longevity of the reaction in different environments. If the pH is higher than 7, then the reaction rate will increase due to the ample amount of hydrogen ions in the hydrogen peroxide. However the pH level cannot be higher than 10 or else there will be too many hydrogen atoms in the peroxide for the enzyme to be able to deconstruct them. If the temperature is increased, then the reaction rate will increase due to the ample amount of energy and movement in the hydrogen peroxide and enzyme.