How Enzymes Affect The Rate Of A Reaction Without Being Used Up

Difference enzymes work better under different conditions. Where in a human body might it be beneficial to have enzymes work in very acidic environments?

Of the many functions of proteins, catalysis is by far the most vital. When catalysis is not present, most reactions in the biological systems take place very slowly to produce at an adequate pace for metabolising organism. The catalysts that take this role are called enzymes. Enzymes are the most efficient catalysts; they can enhance rate of reaction by up to 1020 over uncatalysed reactions. (Campbell et al, 2012).

pH - Enzymes also have an optimum pH level. The pH of a solution affects the enzyme's secondary and tertiary structures. These bonds make the shape of an enzyme's active site. So, if these bonds are broken, the shape of the active site changes and is distorted. If there is no active site, there is no reaction resulting in no products. If the enzyme is put in a pH that is very different from the optimum pH, it can cause the enzyme to denature.

Background and Introduction: Enzymes are proteins that process substrates, which is the chemical molecule that enzymes work on to make products. Enzyme purpose is to increase the rate of activity and speed up chemical reaction in a form of biological catalysts. The enzymes specialize in lowering the activation energy to start the process. Enzymes are very specific in their process, each substrate is designed to fit with a specific substrate and the enzyme and substrate link at the active site. The binding of a substrate to the active site of an enzyme is a very specific interaction. Active sites are clefts or grooves on the surface of an enzyme, usually composed of amino acids from different parts of the polypeptide chain that are brought together in the tertiary structure of the folded protein. Substrates initially bind to the active site by noncovalent interactions, including hydrogen bonds, ionic bonds, and hydrophobic interactions. Once a substrate is bound to the active site of an enzyme, multiple mechanisms can accelerate its conversion to the product of the reaction. But sometimes, these enzymes fail or succeed to increase the rate of action because of various factors that limit the action. These factors can be known as temperature, acidity levels (pH), enzyme and/or substrate concentration, etc. In this experiment, it will be tested how much of an effect

These results shown from this experiment led us to conclude that enzymes work best at certain pH rates. For this particular enzyme, pH 7 worked best. When compared to high levels of pH, the lower levels worked better. The wrong level of pH can denature enzymes; therefore finding the right level is essential. The independent variable was the amount of pH, and the dependent being the rate of oxygen. The results are reliable as they are reinforced by the fact that enzymes typically work best at neutral pH

To improve the results from the experiment buffer solutions that were not whole pHs could have been used e.g. pH 4.5, 5.5 etc. This would have provided more reliable results as a wider range of results would have been produced. Using pHs with decimals would also help to more accurately determine the optimum pH as the optimum may have been above or below the pH stated in the hypothesis; 8. In this experiment however the optimum is taken at 8 because the graph does not rise again.

As stated in the introduction, three conditions that may affect enzyme activity are salinity, temperature, and pH. In experiment two, we explored how temperature can affect enzymatic activity. Since most enzymes function best at their optimum temperature or room temperature, it was expected that the best reaction is in this environment. The higher the temperature that faster the reaction unless the enzyme is denatured because it is too hot. Similarly, pH and salinity can affect enzyme activity.

What other conditions that may affect the action of enzymes? Substrates could affect the action of the

To prevent fluctuation in the pH, a solution known as a “buffer solution” was used in the experiment. Buffer solutions are mixtures of at least two chemicals which counteract the effect of acids and alkalis. Therefore, when a small quantity of alkali or acid solution is added the pH of the enzyme doesn’t change.

Worthington Biochemical Corporation ha put together many different papers on the effects of enzyme action into one paper. It was originally published in 1972 but was last updated in 2013. This article gives a lot of information on the effects of enzyme action that has been seen on many other articles, it shows to be reliable because of the many authors that have been credited. This is a reliable source because these website holds many other useful experiments and general

Introduction: Enzymes are protein catalysts facilitating the conversion of substrates into products (Alexander and Peters, 2011). They go through a whole chemical reaction which starts off with the substrate and then ends up with a product. The only way this reaction can be adjusted or not even work is if they end up going through some sort of affect which only temperature and pH levels can do determining the environment. When enzymes are in an environment that is too acidic or alkaline, their chemical properties, sizes and shapes can become altered (Magher, 2015) Chemical modification of proteins is widely used as a too; to maintain a native conformation, improving stability (Rodriguez-Cabrera, Regalado, and Garcia-Almendarez, 2011) In this experiment, four trials were conducted and recorded every 15 seconds for 5 minutes in order to calculate the optimum levels and IRV.

Enzymatic activity after varying temperatures and pH levels showed that as temperature increased past room temperature and pH levels became too acidic/basic, foam volume/enzyme activity decreased significantly. This supports the hypothesis that enzyme activity will be most reactive at room temperature (25 degrees celsius) and a neutral pH level of 7. Although it worked best at room temperature (25 degrees celsius), it also worked fairly well when the enzyme was placed in ice (0 degrees celsius), rejecting that part of the hypothesis. However, the enzyme was less active at 0 degrees celsius compared to 25 degrees celsius. Catalase activity was minimal to none when the enzyme was heated because the enzyme most likely denatured.

In this experiment, NaOH was the inhibitor used to stop the enzymatic reactions. NaOH is very basic and when added to a solution, will cause a drastic increase in pH, causing denaturation of the enzyme. The amount of product formed could be calculated by placing the test tube in a spectrometer after the addition on NaOH. A spectrometer measures the absorbance of a solution, which helps compare how much of a substance is in a solution.

Most enzyme regulators bind to an allosteric site on the enzyme, and once bound, the shape of enzyme is change, and this can either stimulate or inhibit enzyme activity. In the experiment, the shape of enzyme is changed to increase the rate of cellular respiration when the temperature is increasing until 30C. Once it reaches the optimum point, the enzyme changes to a shape which slows down the activity of cellular respiration. Not only does the temperature affect the rate of cellular respiration, the pH of the sugar solution also affects the rate of respiration. Changes in pH can affect the shape of an enzyme and also change the shape or charge properties of the substrate so that the substrate cannot bind to the active site. To design an experiment to see test the effect of varying the pH of the sugar solution, the materials needed are flask, the liquid varying through acid and base such as lemon juice or the cleaning products, water, balloons, and yeast.

The objective of the lab was to examine the effects of environmental variables on the functions of an enzyme. To the point, an experiment was conducted to test the effect of pH on the function of the enzyme Amylase.