How To Use Enzymes In A Science Fair?

This science fair project explores the role of enzymes in various bodily functions, such as digestion and germ fighting. Enzymes are molecules that help our bodies perform various tasks, such as breaking down food or extracting juice from apples. By studying enzyme kinetics, temperature, and enzyme concentration, scientists can understand how they work and how we can use them to perform decomposition.

Using a potato and hydrogen peroxide, students can observe how enzymes like catalase work to perform decomposition and break down substances. Enzymes are key components of chemical reactions in all living things and can be used in various experiments. Temperature plays a significant role in the effectiveness of the peroxidase enzyme, which converts hydrogen peroxide into oxygen and water.

The project also explores how temperature affects the activity of enzymes in food, such as using fresh or frozen liver as a source of catalase. The activity of the enzyme can change under different temperatures, causing spoilage.

In this cool catalase and hydrogen peroxide experiment, kids put a potato in a jar of hydrogen peroxide to see how catalase acts as an enzyme. Enzymatic activity (catalase enzyme) can be determined by monitoring the enzyme’s ability to decompose hydrogen peroxide into oxygen and water. Enzymes are essential components of chemical reactions in all living things and can be used in science fair projects to explore their functions and applications.

How do you model enzyme activity?

In this activity, you will use a toothpick model to simulate an enzymatic reaction. Your hand will represent the enzyme, the toothpicks are the enzyme’s substrate, and the broken toothpicks are the reaction products. Breaking the toothpicks in half with your hand simulates an enzyme breaking down a substrate.

Can enzymes be reused?

• Enzymes are mostly proteins that catalyze various biochemical reactions. The catalytic reaction occurs through a specific region of the enzyme called the ‘active site’.
• The substrate (S) binds to the active site of the enzyme (E) and forms an enzyme-substrate (ES) complex.
• This transient complex is then converted into an enzyme-product (EP) complex. The EP complex dissociates releasing the product (P) and free enzyme (E).
• Enzymes are reusable. They remain unaltered after the product is released, hence they can be recovered and used repeatedly.

How to calculate enzyme activity?

Enzyme activity= change in OD/time taken (min) x 1/extinction coefficient of enzyme x total reaction volume/ volume of enzyme extrct taken x total volume of enzyme extract/ Fresh wt of tissue (g) x total protein x 1000 = nano moles of enzyme present per g of sample tissue. for catalase ext coff is 39. 4 mM-1cm-1and for peroxidases 26. 6 mM-1cm-1. In case of SOD % inhibition = control OD- treatment OD/ control x 100 =X% inhibition. 50% inhibition is equal to 1 unit of enzyme. then X% is equal to 1/50 x X= Y unit. Calculate activity by inserting value of Y in above formula of activity in place of change in OD w. r. t. time. The rest of formula will be the same.

What are the activities of enzymes?

The Catalytic Activity of Enzymes. Like all other catalysts, enzymes are characterized by two fundamental properties. First, they increase the rate of chemical reactions without themselves being consumed or permanently altered by the reaction. Second, they increase reaction rates without altering the chemical equilibrium between reactants and products.

These principles of enzymatic catalysis are illustrated in the following example, in which a molecule acted upon by an enzyme (referred to as a substrate ( S )) is converted to a product ( P ) as the result of the reaction. In the absence of the enzyme, the reaction can be written as follows:

The chemical equilibrium between S and P is determined by the laws of thermodynamics (as discussed further in the next section of this chapter) and is represented by the ratio of the forward and reverse reaction rates ( S → P and P → S, respectively). In the presence of the appropriate enzyme, the conversion of S to P is accelerated, but the equilibrium between S and P is unaltered. Therefore, the enzyme must accelerate both the forward and reverse reactions equally. The reaction can be written as follows:

How to evaluate enzyme activity?

The study aimed to increase the signal to noise ratio in enzymatic assays by switching the measurement wavelength from 340 to 360 nm. Enzyme activity can be estimated from spectrophotometric data by taking the slope of the linear part of the progress curve resembling the rate of change in the substrate or product monitored. The concentration of the substrate, NADH, can be calculated from the signal intensity using an absorption coefficient. The absorption coefficient of NADH (2. 519 mM −1) was determined by making a calibration curve with varying amounts of NADH prepared under assay conditions.

The overall change in absorbance during the enzyme assay is due to the conversion of NADH to NAD +, which is directly related to the initial amount of NADH through its absorption coefficient. The experimentally determined absorption coefficient of NADH differed from the absorption coefficient calculated from the average difference in absorbance between the start and end of the enzyme assay. This discrepancy was more pronounced for the PDC assay, suggesting some matrix effects occurred in this assay.

The distribution of the specific absorbance of NADH in the ADH assay and the PDC assay is shown in the histograms, based on 404 and 384 samples analyzed for the ADH and PDC assays.

How to win a science fair?

HighlightsChoose An Exciting Topic. Choose a topic that will interest and challenge you. … Learn Cool Theories. After picking a topic, spend a lot of time gathering background research. … Be a True Scientist. … Trudge Onward! … Use Your Brain (it’s not as hard as it seems!)

• Choose a topic that will interest and challenge you.
• Do not be afraid to try something new—you will learn about it along the way.
• Remember that complicated-looking projects do not guarantee a win!

• After picking a topic, spend a lot of time gathering background research.
• Look for important concepts and equations that will explain how and why your experimental results turn out the way they do.
• Find equations that will help you predict the outcome of your experiment. Learn all the important math, physics, chemistry etc. in order to fully understand your project.

• Keep a detailed and up-to-date lab notebook with you regularly.
• It will help you organize your thoughts and if you ever need to go back to see how you did something, you can find out.
• Judges will want to see a lab notebook during the judging period.

How to show enzyme activity?

In general, enzyme activity is demonstrated by fluorescence microscopy as follows. A substrate is offered to the enzyme, which is allowed to act on the substrate to obtain a reaction product which is localized at the site of enzyme activity and is either fluorescent or easily rendered so.

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How are enzymes used in paper?

Enzymes play a crucial role in the pulp and paper industry, particularly in prebleaching kraft pulp. Xylanase enzymes are the most effective for this purpose, and they can also increase pulp fibrillation, water retention, and reduce beating time in virgin pulps. Enzymes can also be used with recycled fibers for deinking, bonding restoration, and increasing freeness. They have special applications in tropical hardwood pulps, reducing vessel picking, selectively removing xylan from dissolving pulp, and retting flax fibers.

Blenching is the removal of lignin from chemical pulps for aesthetic and paper properties. Current bleaching methods use large amounts of chlorine and chlorine chemicals, which can cause harmful byproducts. Enzymes offer a simple and cost-effective solution to reduce the use of these chemicals and achieve a higher brightness ceiling. Two enzyme-based approaches have been investigated: hemicellulase enzymes and ligninolytic enzymes. Hemicellulase enzymes are commercially used in pulp bleaching, with endo-β-xylanase being the main enzyme needed for delignification. Ligninolytic enzymes, produced by white rot fungi, are more effective in bleaching kraft pulps.

What are some fun facts about enzymes?

Enzymes are very temperature-specific. They get damaged at high temperatures which are above 40 degrees celsius.

Enzymes play an important role in the digestion of food in our body. They are found in the saliva, pancreas, stomach, and small intestines.

Enzymes are even used in industries such as food processing, paper industries, and detergents.

Enzymes are also pH specific. pH around the enzymes can affect their reaction rate.

How to do a science fair project step by step?

Scientific MethodStep 1: Determine the problem or question. In this step you decide what it is that you will study. … Step 2: Develop your hypothesis. … Step 3: Design an experiment to test your hypothesis. … Step 4: Conduct your experiment and collect the data. … Step 5: Draw Conclusions from your data.

The Maine State Science Fair welcomes research or engineering projects in any of the following general categories.

• Animal Sciences
• Behavioral and Social Sciences
• Biological Sciences and Engineering
• Biomedical and Health Sciences
• Chemistry and Materials
• Computer Science
• Earth and Environmental Sciences and Engineering
• Energy and Transportation
• Engineering Mechanics
• Mathematical Sciences
• Microbiology
• Physics and Astronomy
• Plant Sciences

Project Development. Anyone who has read a mystery novel or seen a “whodunit,” has seen the scientific method in action. It is a logical, organized mechanism for identifying and researching a problem and devising a strategy to solve it. There are 5 major steps of the scientific method.

How do scientists use enzymes in research?

Researchers have been using restriction enzymes to manipulate, analyze, and create new combinations of DNA sequences since the early 1950s. In the 1950s, researchers Salvador Luria and Joe Bertani discovered that some bacteria were more resistant to viral infections than others, known as bacteriophages. These viruses infect bacterial cells and aim to produce more by injecting their genome into a host cell, copying it, and expressing bacteriophage genes. However, some strains of bacteria appeared less vulnerable to bacteriophage infections and resisted the hijacking of their cell machinery by bacteriophages.

The discovery of restriction enzymes began with a hypothesis by Werner Arber in the 1960s. He hypothesized that bacteriophage-resistant bacterial cells might express two types of enzymes: a restriction enzyme that recognizes and cuts up the foreign bacteriophage DNA and a modification enzyme that recognizes and modifies the bacterial DNA to protect it from the DNA-degrading activity of its own restriction enzyme. This prediction was confirmed in the late 1960s by Stuart Linn and Arber when they isolated a modification enzyme called methylase and a restriction enzyme responsible for bacteriophage resistance in the bacterium Escherichiacoli.

Hamilton Smith in 1970 verified Arber’s hypothesis and elaborated on the initial discovery by Linn and Arber. He successfully purified a restriction enzyme from another bacterium, Haemophilus influenzae (H. influenzae), and showed that it cut DNA in the center of a specific six-base-pair sequence. Dan Nathans and Kathleen Danna later used Smith’s restriction enzyme to cut the 5, 000 base-pair genome of the SV40 virus, which infects monkey and human cells, and identified eleven differently-sized pieces of DNA. This method of cutting a DNA molecule into smaller pieces became a powerful tool for generating physical maps of a multitude of genomes, which was a precious revelation in the early stages of genome sequencing.