Catalase Experiment

An enzyme is s specialized protein made to catalyze a chemical reaction. Enzymes form a complex with a substrate and break the substrate down to chemical products far more quickly than the random chemical reactions that would have occurred without the enzyme. In this experiment we were testing to see how different factors of enzymes would effect the rate that they broke H202 into H20+02. Measuring the amount of O2 with guaiacol to see how orange the solution turned showing the rate of the enzyme break down. The hypothesis of this experiment was supported in some of the results that came from each factor experiment. The concentration rate hypothesis was supported by the results that the enzyme absorption does increase as the concentration increases.

The three things that can cause the enzyme to denature is a large change in pH level, High Temperature, and substrate concentration. According to our knowledge, we know that a large change in pH will cause instability in the protein structure thus resulting in denaturation of the enzyme. From the data, we can see that pH 3 (total:6.3) and 10 (total:6.2) were the slowest because pH 3 is probably the highest acid and pH 10 is the highest base. The highest acid or base pH represents a large change which would cause the enzyme to denature. The fastest pH was 6 (total:34.5), and it seems that there wasn’t a large change which resulted in a stable structure. The temperature in our experiment was not very high which didn’t result in denaturation of peroxidase. The temperature seemed to be a constant that didn’t affect the experiment. If the temperature was higher in pH 3 and low in pH 10, then it would cause pH 3 to denature even more which would make the pH 3 total about 4.0. Substrate concentration basically means the amount used for the substrate. The substrate in our experiment was 0.1% hydrogen peroxide. The 0.1% is the concentration amount. Just like temperature and pH, substrate concentration can speed the reaction only up to a certain limit. When we mixed pH 3 enzyme tube with substrate tube, we used 0.3 mL of hydrogen peroxide, but if we were to increase the amount, then the experiment would have been faster. Our

the propose of this experiment was too see if the chemical reaction of a enzyme can be made faster.

Chemical reactions are seen in many instances, including those in which one substance is being converted to another. Natural chemical reactions will occur without intervention, however they occur slowly. Enzymes become important in these situations. Enzymes are proteins that act in cells to ensure reactions occur at appropriate speeds. In other words, they act as catalysts. Catalysts are chemicals that can be added to these reactions to increase the rate of the reaction without being changed or consumed. Enzymes act upon specific molecules called substrates. The relationship between enzymes and substrates can be thought of as a lock and key relationship. Every substrate has a specific enzyme that can act upon it and change it.

What will happen if the temperatures are not right on the day we investigate the investigation?

Figure 1 shows that the optimum temperature for catalase to catalyze hydrogen peroxide is around room temperature (30℃) as it has a very fast reaction rate (5). The overall trend is that temperatures that differ from 30℃, will decrease the reaction rate.

The purpose of quantitative analysis of protein using a spectrophotometer is to measure the concentration of proteins in a given sample. The experiment is conducted by laboratory method (Biuret Test) and using spectrophotometer to analyze the absorbance of reactants at 540 nm, hence determining the concentration of the proteins in a given sample.

Enzymes are biological catalysts that increase the rate of a reaction without being chemically changed. Enzymes are globular proteins that contain an active site. A specific substrate binds to the active site of the enzyme chemically and structurally (4). Enzymes also increase the rate of a reaction by decreasing the activation energy for that reaction which is the minimum energy required for the reaction to take place (3). Multiple factors affect the activity of an enzyme (1). These factors include the pH and the temperature of the solution (1). Most enzymes have a preferred temperature and pH range (2). The preferred temperature for catalase falls between the ranges of thirty five to fifty degrees Celsius (4). Temperatures that are too high denature the enzyme and halt the enzyme’s activity (2). Catalase denatures starts to denature at fifty five degrees Celsius (2). Reactions in the human body produce hydrogen peroxide as a product (1). Since hydrogen peroxide is poisonous to the human body, catalase catalyzes hydrogen peroxide into water and oxygen (2 H2O2 → 2 H2O + O2) (1). According to the collision theory, a reaction can only occur if particles collide with sufficient energy to overcome the activation energy and with correct geometrical orientation (3). Increasing temperature increases the kinetic energy of the particles which means that an increase in temperature will increase the speed of the hydrogen peroxide and the catalase molecules which

The purpose of this study is to investigate the effects of varying the concentration of peroxidase on rate of reaction, as well as, the varying temperature and pH levels. Enzymes are proteins that catalyze biochemical reactions that work by reducing the activation energy for each reaction, causing an increase to the rate of the reaction. One class of enzymes are known as peroxidase. Peroxidase catalyze the oxidation of a particular substrate by hydrogen peroxide. Meaning that it eliminates H2O2 in order to prevent damage to the cells and tissues (Department of Biology University of Tampa 74). Peroxidase is the most reliable and accessible enzyme to use as it can be easily prepared and tested (Ramesh Kumar 1). An enzymes shape is critical

Enzymes are proteins that significantly speed up the rate of chemical reactions that take place within cells. Some enzymes help to break large molecules into smaller pieces that are more easily absorbed by the body. Other enzymes help bind two molecules together to produce a new molecule. Enzymes are selective catalysts, meaning that each enzyme only speeds up a specific reaction. The molecules that an enzyme works with are called substrates. The substrates bind to a region on the enzyme called the active site. The active site is precisely shaped to hold specific substrates.

Enzymes are “proteins that help lower the energy necessary to do chemical reactions within the body”. They are considered biological catalyst. When the environment changes, the ability of an enzyme to catalyze a reaction decreases. Very high temperatures can denature enzymes by destroying their bonds and their shapes. Low temperatures, can cause enzymes to slow down and decrease their rate of interaction with substrates. The structure of an enzyme are chains of amino acids, and have a specific shape that allow chemicals to react with the enzyme. Enzymes are natural atoms that altogether speed up the rate of essentially all of the chemical reactions that take place inside cells. A lab was conducted to test the effects of different diets on enzyme

In this experiment we tested If the increase or decrease in enzymes affect the digestion rate of the substrate. Enzymes are proteins that are very important for all organisms. enzymes are very efficient catalyst for specific chemical reaction. Their purpose is to allow the cell to carry out chemical reaction very quickly so that the cells can build things or take things apart. all enzymes are unique in their own way. different enzymes have different active sites. the active site of an enzyme is where the molecules attached and are either broken apart or put together. The active site binds to substrate based on many different factors like shape stereochemistry electrical charge and hydrophilic and hydrophobic. the enzyme used in

ABSTRACT: The purpose of the experiments for week 5 and week 6 support each other in the further understanding of enzyme reactions. During week 5, the effects of a substrate and enzyme concentration on enzyme reaction rate was observed. Week 6, the effects of temperature and inhibitor on a reaction rate were monitored. For testing the effects of concentrations, we needed to use the table that was used in week 3, Cells. The 3 concentrations of enzymes were 0.5 ml, 1.0 ml, and 2.0 ml of turnip extract, while the substrate consisted of 0.1ml, 0.2 ml, and 0.4 ml of hydrogen peroxide. In a separate tube, the control was made up of turnip extract and guaiacol, known as the color reagent. This was recorded the absorbance every 20 seconds for 3 minutes.

Drug companies must apply the knowledge gathered from the effects of substrate concentration in an enzyme catalyzed reaction. The awareness of inhibitors must be applied so that their developed drugs do not inhibit enzymes. It would be important to consider substrate concentrations in relationship to target enzymes that are exposed. Competitive inhibitor drugs compete with high concentrations of ATP in the cell and proteins inside the cell contain lower concentrations. Thus the knowledge of the effects of substrate concentration on enzyme activity would aid drug designers in utilizing competitive inhibitors that will inhibit the enzyme more effectively. The essentials of enzyme activity and total change were tested in being exposed

Bio Chem lab Report 04 Enzyme Biochemistry Group Member: Chan Man Jeun Duncan (16002621) Law Sze Man (16000478) Introduction Enzyme is a protein base structure substance in our body. It works at a biocatalyst that will catalyzing the chemical reaction, which helps to speed up the chemical reaction. Enzyme could only function in specific shape, and the shape of enzyme is depending on the environment, therefore it is hard for an enzyme to function well in an extreme environment. The aim of this experiment is to see can the enzyme functions normally in different environment(pH, temperature and salt concentration) via using starch solution, amylase from saliva, 0.5M HCl solution, 0.5M NaOH solution and NaCl solution, and using iodine solution