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  1. Introduction
  2. Materials and Methods
  3. Discussion
  4. Conclusion

When talking about enzymes, also known as proteins, you are talking about 3-dimensional structures in your body that act as catalysts, which speed up chemical reactions. If enzymes did not exist in our body these chemical reactions would be occurring at a slow enough rate to where our body would not be able to function on a daily basis. (G. Karp, 2010) Every enzyme is different and has a specific role they function in. For example, the enzymes located in our gut help break down the larger molecules into smaller ones, as opposed to the enzymes that assist in making DNA, which uses small molecules to form large characterized ones.

Every enzymes unique shape accommodates the structure of the substrate. The enzyme acts on the substrate molecule forming the product known as the enzyme-substrate complex. The uniquely shaped substrate binds to the enzyme through the active site. Every active site only allows certain substrates to bind to it, but once bonded the enzyme will then convert the substrate molecule into product.

The enzymes function is determined by the enzymes shape and structure, and if any alteration were made to the structure it will have denatured the enzyme causing it to lose its primary function. Enzyme activity can be affected by extreme changes in environmental conditions. Some of these conditions include temperature, pH, enzyme concentration and substrate concentration. (D. Voet, J. Voet, C. Pratt, 2013) The Michaelis-Menten model equation shows the relationship between the rate of the reaction and its substrate concentration. Understanding how this equation works puts together the logic of how enzyme kinetics functions.

[...] This experiment showed how the enzyme is affected with time with no environmental factors affecting it. The protocol did a well job showing that as time increases so will the concentration of the product. The temperature experiment supported the original hypothesis stating if we raised or lowered the temperature outside the enzymes optimal temperature at it will cause the enzyme to break down and denature, making it lose its function. When you raise the temperature of the enzyme you increase its kinetic energy as well. [...]

[...] Understanding how this equation works puts together the logic of how enzyme kinetics functions. The protein structure is based on hydrogen bonding and dipole-dipole interactions between amino acids. A change in pH can disable the amino acids from forming hydrogen bonds or dipole-dipole interactions, which will in turn affect the structure of the enzyme, leaving it denatured. A change in pH can also affect the amino acids in the active site because when the shape changes, the substrate will no longer be able to fit with the active site making the enzyme lose its primary function which is fatal for an enzyme.(Biotechnology Explorer Team's) In this lab experiment, the enzyme being tested is cellobiase. [...]

[...] Graph Temperature This graph represents Vo versus temperature forming somehwhat of a bell curve. The optimal temperature point is located at 37 C. It is easy to observe the increase in the rate of the reaction as the temperature is raised reaching the optimum, and then lowering as the temperature is extremely increased. Table pH This table lists the absorbance gathered for each level of pH by the spectrophotometer. The concentration obtained by the standard curve is listed as well as the different levels of pH chosen for this experiment. [...]

[...] So the deeper the yellow the more product formed. If your product is a faint yellow or clear then little to no product was formed. It is also more economically efficient working with an artificial substrate because we would have to obtain large quantity amounts of the cellobiose to form a useable product for the spectrophotometer. (Biotechnology Explorer Team's) In this experiment a total of five hypothesis were predicted as a guide to determine and understand the outcome of this experiment. [...]

[...] Pratt (Fundamentals of Biochemistry) T. [...]

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