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. [...]
[...] It then becomes inactive and being unable to take further part in any reactions. According to the bell curve graph when we set the temperature to and 25°C you could see an increase in the rate of the reaction reaching the maximum rate when set to its optimal temperature at 37°C. The curve then decreases extremely, when the temperature is set at 100°C. So as the temperature increases the rate of the reaction will also increase due to a rise in the kinetic energy. [...]
[...] A bell curve was constructed having an optimal pH at 5. Lowering or raising the pH of the optimum affects the rate of the reaction, Vo. Table Enzyme Concentration This table lists the absorbance and concentration collected from the standard curve. The Vo was collected when the concentration versus time were plotted. The enzyme concentration was collected from the protocol. Graph Enzyme Concentration The graph represents concentration versus time at a set enzyme concentration. The more enzyme concentration added the more product produced. [...]
[...] This experiment follows the enzyme concentration, except that when you reach the maximum possible point where the enzyme is saturated with the substrate there will no longer be a rise in reaction and it will remain in a stead state. (T. Sheppard, 2005) Overall, every experiment conducted supported each predicted hypothesis for it. A better understanding of the different factors that can affect enzyme activity such as; temperature, pH, enzyme concentration, substrate concentration and time was acknowledge. References: Biotechnology Explorer Team's Biofuel Enzyme Kit G. Kaiser (http://student.ccbcmd.edu/~gkaiser/biotutorials/proteins/enzyme.html) G. Karp (Cell and Molecular Biology) D. Voet, J. Voet, C. [...]
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