Enzyme has an active site in a specific shape because of its tertiary structure. Enzyme works for binding with substance of a specific shape that fits in it and break down the substance. Enzymes denature due to various factors. The temperature, PH level, and the concentration of the substance influence enzyme activities. When these factors vary, enzymes may change in shape so it will not be able to bond to the specific substance anymore.
I chose to do an experiment on ‘How temperature can affect the rate of enzyme activity in the liver?’ Temperature affects the “speeds of the molecules, the activation energy of the catalytic reaction and the thermal stability of the enzyme and substrate.” (2) At different levels of temperature the affects on the enzyme in the liver varies. The reason for this is because; “their molecules have low kinetic energy and collisions between them are less frequent.” (2) In other words at low temperatures, enzymes become ‘deactivated’. (2) Whereas on the other hand when the temperature is increased the activity that occurs in the
Enzymes are proteins that are used to speed up these reactions without being consumed by them. The activity of these enzymes can be altered by changing their environments, such as enzyme specificity (speed only a reaction that contains their substrate), increasing and decreasing temperature, concentration level, or adjusting the pH level. Catalase is a catalyst that digests potent hydrogen peroxide and converts it into H2O and O. It is due to this hydrogen peroxide digesting ability that we used catalase in this experiment. To record the role that environment plays in the reaction of an enzyme, we exposed the enzyme to various changes in temperature, concentration, and pH.
If the PH goes over the optimum PH then the chemical nature of the amino acids can alter. This may cause the bonds that hold the tertiary structure together to break. The active site will be disrupted and the enzyme will be denatured. Substrate concentration - At low substrate concentrations many active sites will not be occupied, decreasing the rate of reaction. At high substrate concentrations most to all of the active sites will become occupied, increasing the rate of reaction.
Effect of Enzyme Activity on Temperature Aim: The aim of this experiment is to investigate how effectively the enzyme amylase breaks down starch at different temperatures Research Question: How does the increase in temperature affect the time taken for amylase to breakdown 2ml of starch? Purpose: Background Information: Enzymes are biological catalysts that comprise the largest and most highly specialized class of protein molecules. Enzymes act as catalysts to increase the rates of chemical reactions. A fundamental property of enzymes is their specificity. Various enzymes have unique shape and chemical composition that creates a site, called and active site.
Hydrogen peroxide is also a dangerous, very potent by-product of metabolism, so it is essential that it is broken down quickly, otherwise it would cause damage to cells. Hypothesis I believe that as the concentration of the hydrogen peroxide (substrate) decreases, the rate of reaction will decrease consequently. This is because there will be fewer collisions between the substrate and enzyme molecules (catalase in yeast) – because there are fewer molecules of hydrogen peroxide, so there will be a decrease in enzyme-substrate complexes formed. The reaction will then stop because all of the active sites become saturated with substrate because the enzyme is the limiting factor. This will result in a decreased volume of oxygen being produced as one of the by-products of this reaction.
These fermentative bacterica produce an acidic environment within the tank. These bacteria will further break down the material into ammonia, H2, CO2, H2S, and shorter volatile fatty acids,but alas it is still too big for methane production! So, we go to our next stage to help break it down more. This process is called Acetogenesis. Acetogenesis is the creation of acetate, which is a derivative of acetic acid.
Enzymes and proteins are affected by the same factors Enzymes are biological catalysts; they increase the rate of chemical reactions without being used up. Enzymes are proteins that are shape differently to allow the substrates to fit inside of them, the place where the substrates fit is called the active site. If the shape of an enzyme changes, the active site might not work, the changing of the shape is called denaturing. Enzymes can not be killed, although they are made by living things they are proteins and are not alive Enzymes can be denatured by high temperatures or high levels of pH. Enzymes and temperature As the temperature increases, so does the rate of reaction, but very high temperatures denature enzymes.
Discussion: The proteins solubility can be determine based on the salt concentration in the solution in a way that when the concentration is low, various charged groups on a protein molecule will be stabilized by the presence of salt. This actually attracts the protein into the solution and the solubility of protein is enhanced which is generally known as salting-in process. On the other hand, as the concentration of the salt increases, the point of maximum solubility of the protein is reached and cause the increase in salt concentration which suggest that there was less water available to solubilise the protein. As the water interaction become less marked, the protein-protein interactions became more important causing the protein to aggregate and come out of solution. This protein precipitation in the presence of excess salt is also known as salting-out process.
Catalase Lab Report Introduction Enzymes are proteins that speed up the rate of reactions that would otherwise happen more slowly. Enzymes work by fitting into certain substrates to lower the energy needed for the process to work. This is similar to the lock and key. The key being the substrate and the lock being the enzyme. If the substrate (key) doesn’t fit it won’t work with the enzyme (lock).