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.
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).
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.
This protein precipitation in the presence of excess salt is also known as salting-out process. In this experiment, ammonium sulphate was used for the salt fractionation process. Ammonium sulphate was used especially for salt fractionation due to its high solubility and it is relatively inexpensive. Enzyme purification can also be carried out by following the same set of methodology as those for protein since enzyme is protein. However, some attention such as permanent loss of activity must be put into consideration due to denaturation under unfavourable conditions.
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
Deficiency of phenylalanine causes numerous healthy problems such as altered state of mind, lack of energy, memory issues, confusion, and decreased alertness. High blood levels of phenylalanine can also be bad. High levels of phenylalanine can lower intelligence, causes anxiety and depression, and the inability to focus or pay attention. This is why phenylalanine is such an important molecule. Too much of it can cause problems and a deficiency also causes health problems, therefore it is important to be educated about it.
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.
Once these two components come together, certain chemical bonds within the substrate molecule change much as a lock is released, and just like the key in this illustration, the enzyme is free to execute its duty once again. Many chemical reactions do proceed but at such a slow rate that their progress would seem to be imperceptible at normally encountered environmental temperature. Consider for example, the oxidation of glucose or other sugars to useable energy by animals and plants. For a living organism to derive heat and other energy from sugar, the sugar must be oxidized (combined with oxygen) or metabolically "burned" However, in a living system, the oxidation of sugar must meet an additional condition; that oxidation of sugar must proceed essentially at normal body temperature. Obviously, sugar surrounded by sufficient oxygen would not oxidize very rapidly at this temperature.
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.
Various enzymes have unique shape and chemical composition that creates a site, called and active site. This is to allow connection between the enzyme and other molecules called substrates. The shape and chemical makeup of the active site provides an area for part of the substrate to connect with the enzyme. (Farabee, 2010) Part of the active site holds the substrate and part catalyzes the reaction. Some enzymes act on one substrate only, while other enzymes act on a family of related molecules.