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.
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.
Digestive enzymes are hydrolytic enzymes. Their substances, or the molecules on which they act are organic food molecules which they breakdown by adding water to the molecular bonds, thus cleaving the bonds between the subunits or monomers. Digestive enzymes can function outside the body cells; their activity can be studied by test tubes (Marieb and Mitchell 2010). This experiment attempts to re-create the breakdown process that is normally done via digestion with Iodine as a vital component. It can be expected that once amylase reacts with the starch, maltose will then be broken down and less starch will be visible and more sugar will be apparent thus causing the solution mixed with iodine to become lighter and lighter.
The reason for this is because; this allows the substrate to bind to the active site, which is known as the ‘lock and key model’. The substrate is the key and active site is the lock. No other key will fit into the lock. There are many factors that affect the rate of enzyme activity in the liver, namely, Ph level, and substrate concentration. 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.
However, some attention such as permanent loss of activity must be put into consideration due to denaturation under unfavourable conditions. In the first procedure, saturated salt solution was added slowly to the protein mixture to bring up the concentration of the salt of the mixture. The precipitated protein was collected and categorized based on the concentration of the salt solution at which it is formed in which it is called as fractionation. As a result, the protein fractions that were collected at the earlier stages of addition of the salt are less soluble in the salt solution than the fractions that were collected later after that (Spadaro, 2003). This can be seen from
If the substrate (key) doesn’t fit it won’t work with the enzyme (lock). This is important because without enzyme the processes would be to slow and poisonous chemicals would build up. The factors that affects if an enzyme would work correctly or not is if there is a suitable pH level and temperature. An example of an enzyme is Catalase. It is the one that we used in our experiment.
1 mark AND Extreme pH denatures the enzyme, altering the shape of the active site and preventing the enzyme and substrate forming a complex, thereby decreasing the rate of the reactions. This is seen in a decrease in the amount of oxygen being produced. 1 mark c. This pH will need to be read from the graph 1 mark AND Optimum pH 1 mark Question 2 a. Any 2 of the following The volume the pH solution The volume of peroxide The surface area of the liver cube The same size test tube 1 mark b. The pH 1 mark c. Treatment group refers to all groups which are being manipulated or varied during an experiment.
Enzymes, as a subclass of catalysts, are very specific in nature. Each enzyme can act to catalyze only very select chemical reactions and only with very select substances. An enzyme has been described as a "key" which can "unlock" complex compounds. An enzyme, as the key, must have a certain structure or multi-dimensional shape that matches a specific section of the "substrate" (a substrate is the compound or substance which undergoes the change). 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.
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.
On the surface of the enzyme is an active site that temporarily binds the reactants or substrates forming an enzyme-substrate complex. The catalytic action of the enzyme then converts the substrate to a product or products. This conversion can take the form of a synthesis (building more complex molecules), a decomposition (splitting of the substrate), an oxidation/reduction (addition or removal of electrons), or an isomerization (rearrangement of atoms within a molecule). When the product or products are released, the enzyme emerges unchanged and available to convert more substrate into more products. Since enzymes can be used again and again, they are effective even at low concentrations.