Create a 5 pages page paper that discusses tyrosinase in the experiment. This study will explore one dynamic trait of enzymes which is the enzyme kinetic description. In many cases, the reactions that

Create a 5 pages page paper that discusses tyrosinase in the experiment. This study will explore one dynamic trait of enzymes which is the enzyme kinetic description. In many cases, the reactions that are catalyzed by enzymes follow an ES complex format shown in equation 1.

E9E +S ES E + P, where E is the enzyme, P is the product, and S is the substrate (Kumar, C. 2011). For an enzyme that is specific, one substrate molecules may bind in the required way to give out a function of the EES complex. On the other hand, the substrate needs to have a shape, size, and polarity that is compatible with the active enzyme site (Witkop, C. 2009). Other enzymes may catalyze the many different molecules transformation whenever there exists a common category of a chemical linkage of the given substrate. Some have specificity hence can form ES complexes that are reactive having one structure of a molecule.

The first velocity of reaction (V0) of a reaction catalyzed by an enzyme is variable in accordance with the concentration of the substrate (s). The Michaelis Menten equation was established to account for the kinetic properties of the different enzymes. This equation is given as. V0 = JTK.

The reagents were dissolved in the phosphate buffer. These reagents included a combination of enzyme, phosphate buffer, an inhibitor of the specific experiment and the substrate. The required phosphate buffer volume was pipetted together with the substrate and the inhibitor into the cuvette. The solution was well mixed and the colorimeter on the cuvette zeroed. The cuvette was removed from the colorimeter. The needed volume of the enzyme was quickly added and mixed through covering the cuvette using paraffin. The stop clock was then started. The cuvette was placed in the colorimeter and the initial reading taken at fifteen seconds. The recording process continued at an interval of fifteen until two minutes. The final cuvette volume of the experiment was 3.0 cm cubed. To determine a suitable tyrosinase concentration for the analysis of the kinetics, the experimental set up was set up and ran as displayed in table 1. The volume of the enzyme was varied whereas the substrate was kept constant.