Importance of Enzymes as Catalysts - Lab Report Example

Importance of enzymes as catalysts Enzymes play a significant part in altering the reaction rate in all biological reactions, where they are present. Mostly, enzymes are in form of proteins in nature. By altering the reaction rate, it means that they either slow or make fast the rate of reaction. Proteins fundamentally act as enzymes which enhance the rate of reaction inside the cells. Most biological reactions are altered or catalyzed by enzymes (proteins). Without enzymatic catalysis, reactions that are biological would not take place because they are so slow in nature, especially under temperature conditions that are mild and pressure that makes them compatible with life. Enzymes do accelerate reaction rate by more than 1 million g=folds, in that reactions would take a very long time to occur. Appropriate enzymes catalyze in few seconds and there activities, in many cases occur inside the cell, within the membranes of the cell. The rate of reaction when Ph, temperature, time and the substrate are at a constant is determined by the enzyme availability. Effects of enzymes in substrate concentration can be analysed as below. The concentration of enzymes is a factor in determining the rate of reaction. The substrate needs to be present in excess. That is to say that each reaction should be independent of the concentration of the substrate. Any possible change in product amount over a given time period depends upon present enzyme level. Explain Michaelis-Mentan equation and the constants A and E reacting leads to B at a constant rate k1, this turns to C and generates E again at a constant rate k2. At that instance, B has the possibility of turning into A and E again at a constant rate k-1. Michaelis-Menten enzymatic catalysis mechanism follows this path. There are no analytical solutions to the equations but numerical solutions might be available. The steady state approximation may be significant in giving the expression below for reaction rate. where KM is referred to as the Michaelis Constant. Competitive and uncompetitive inhibitors of reaction Competitive inhibition has a molecule similar to the present or available substrate but not able to be acted on by those enzymes that compete with them for sites that are active. Fewer active sites readily act on the substrate because of the inhibitor presence. Given the structure of the enzyme is not affected by the enzyme inhibitors; they will still act as catalysts for the reaction. In inhibition that is uncompetitive, molecules tend to bind to enzymes instead of sites that are active. That makes the three dimensional enzyme structures to change in that its site that is active still binds to the substrate in affinity that is usual, though not in the optimal arrangement of stabilizing the rate of transition and in turn catalyzing the reaction. Purpose of lineweaver burk plots Lineweaver Burk plots are significant in a number of ways. For instance, in the case where it is used in enzyme inhibition determining, the lineweaver-Burk plot differentiates between competitive non, and uncompetitive inhibitors. Graph analysis If I was to obtain a CIAP preparation giving a lower specific activity of catalysis than 2.317 microgram/min, I would conclude that the new preparation has lots of impurities that did lower the reaction rate. More so, I would consider that as lack of an active site and a catalyst to work on the site in ensuring that the reaction rate is high and fast. What would you conclude about the relative purity of the new preparation? The new preparation has lots of impurities making the reaction rate slow down. Effect of enzyme interaction at PH of 8 and PH of 11 In the case where any enzyme is submitted to a high PH that denatures it, automatically, there will be no enzymatic activity taking place. Enzymes at the PH of 11 might get denatured and fail to support any activity of the enzymes. More so, those enzymes at PH of 8 will react better than PH of 11 and the reaction may be steady. Very high PH is not good for the structure of an enzyme given it eats it up leading to the denaturing aspect. If an enzyme is submitted to a pH level under which it is denatured there will be no enzymatic activity. Despite the fact that most enzymes react well between the pH of 6 and 8, pepsin functions best at a PH of 2 while trypsin works appropriately at PH of 8. What causes the reaction of rate to decrease when performed on ice at 65 degrees Celsius? The ice has a higher affinity of absorbing heat from given it is cold. The temperature that would have been sufficient in carrying out the experiment or reaction activity goes to the ice instead of the reaction elements. On the other hand, It is significant to, at molecular level, assay enzymes at a temperature that is optimum. This is done to avoid the enzymes from denaturing in cases where the temperatures are too high. The sodium phosphate speeds up the reaction and raises the Km and the Vmax of CIAP. Typically, uncompetitive inhibitor will relay such effects in a reaction. It covers the active sites of the substrates and hinders the reaction from taking place well. The L-phenylanine affects Vmax and KM of CIAP by making them progress in the reaction without much inhibition. The inhibitor in this case is the noncompetitive inhibitor. Enzyme characterization is useful and significant in industrial research given the fact that it is used in determining pathophysiology in proteomic research Conclusion In conclusion, enzymes are very significant when it comes to making fast and lowering or making slow the rate of reaction. They work well when put in optimum temperature and other favorable conditions needed for the survival of the enzyme. They might get denatured making them inactive and unable to perform the reaction role or rather the catalyzing role in the reaction. There characterization and up to industrial research given the fact that it has significance in pathophysiology and proteomic research. Work Cited Perry, James W, David Morton, and Joy B. Perry. Laboratory Manual for General Biology for Starrs Biology Texts. Belmont, Calif.: Thomson Brooks/Cole, 2007. Print Read More