Catalase Enzyme Activity Analysis

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.

peroxide (H2O2). The enzyme breaks H2O2 into water and oxygen. The production of the oxygen

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.

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,

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

With all living organisms, a process known as cell respiration is integral in order to provide the body with an essential form of energy, adenosine triphosphate (ATP). Oxygen, although an essential part of this process, can form reactants from colliding with electrons associated with carrier molecules. (pb101.rcsb.org, 2017). Hydrogen peroxide is an integral product of this reaction but is known to impose negative effects on the body if high levels are introduced. Explicitly, this reaction is caused “If oxygen runs into (one of these) carrier molecules, the electron may be accidentally transferred to it. This converts oxygen into dangerous compounds such as superoxide radicals and hydrogen peroxide, which can attack the delicate sulphur atoms and metal ions in proteins.” (pdbh101.rcb.org, 2017). Research has suggested that the hydrogen peroxide can be converted into hydroxyl radicals, known to mutate DNA, which can potentially cause bodily harm due to DNA’s role in the synthesis of proteins. These radicals can cause detrimental effects on the human body, and studies have suggested a link to ageing. Due to the harmful effects of these H2o2, it is important that the body finds a way to dispose of hydrogen peroxide before concentrations are too great.

An Enzyme is a protein that in essence speeds up biological reactions. So that would mean that a Catalase is an enzyme reaction that decomposes hydrogen peroxide to water and oxygen. It is primarily found in the liver and it is important in protecting the cell from damaging oxidative reactions.

Peroxidase is an enzyme that breaks down hydrogen peroxide in our cells (Bansal et. al., 2016). Peroxidase is essential in life because hydrogen peroxide can cause damage to the cell. Hydrogen peroxide is the substrate to the peroxidase enzyme, where it binds to the active site and is broken down into water. In order to monitor the breakdown of hydrogen peroxide, the colorless dye guaiacol binds to the peroxidase and becomes oxidized as hydrogen peroxide is reduced to water, which then turns brown. Hydroxylamine is an inhibitor that has a similar structure to hydrogen peroxide. When hydroxylamine binds to the active site of peroxidase, it inhibits hydrogen peroxide from binding, thus preventing the breakdown of hydrogen peroxide (Lab Handout,

When we’re young, our cells have a very strong defense system known as superoxide dismutase (SOD) that kicks free radical butt. But as we get older, SOD doesn’t work as well. Without SOD keeping the peace, the free radicals have a field day and wreak as much damage as they possibly can causing our cells, and eventually us, to die. Free radicals have also been linked to a number of diseases such as cancer, dementia and heart disease.

Observing how the enzyme catalase found in chicken and beef livers breaks down hydrogen peroxide at varying pH levels and temperatures.

Within a cell, enzymes are used as a catalyst to increase the rate of chemical reaction. They do not consume themselves, rather they help in increasing the rate of reaction. Within the body, enzymes vary depending on their specific functions. For instance, hydrogen peroxide is a toxic chemical, but it breaks down into harmless oxygen and water. This reaction can be sped up using the enzyme catalyst produced by yeast. Hydrogen peroxide is produced as a byproduct in cellular reaction, because it is poisonous and must be broken down, therefore this reaction is important. The speeding up of the reaction is shown below:

reaction rate increases. If the temperature of an enzyme gets to high the reaction rate will slow

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.