BIOL ENZYME REPORT

BIOL ENZYME REPORT - Observing the enzymatic activity of...

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Observing the enzymatic activity of catechol oxidase: When subject to various temperatures and in the presence or absence of a co-factor. Nisel Desai June 2, 2008 TA: J. Lande Section 405 BIOL 101L
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Appendix of Figures Figure 1: Data Table below bar graph that displays recorded measurements of absorbance values. Figure 2: Line graph that sisplays change in absorbance values that are adjusted using a formula that is calculated in Table 1.
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Table 1: Displays detailed calculation of adjusted values for part I of experiment Data and Calculations of Part I Cuvette Initial Absorbance Final Absorbance (10 Min) Final A - Initial A Calculation explained: n is equal to the differences in absorbance value over time: ( Final A - Initial A) n minus the previous data point, or n+1 is equal to the baseline correction value for every two data points For example: let n= -0.097, which is the difference in absorbance over ten minutes of the contents in cuvette 1 let n+1= -0.121. (n+1) - (n) = the baseline value= -0.218 Calculated Values 1 0.274 0.371 -0.097 0.218 2 0.41 0.531 -0.121 0.37 3 0.419 0.187 0.232 0.434 4 0.37 0.508 -0.138 0.508 5 0.574 0.352 0.222 (these are the values displayed in Figure 3) 6 0.306 0.518 -0.212 7 0.454 0.184 0.27 8 0.314 0.557 -0.243 9 *calibration 0.274 0 0 Figure 3: Bar graph that indicated the specific inhibition of the cofactor of catechol oxidase in part II of experiment. As well as change s in absorbance over time.
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Introduction: The absence of enzymes in organisms would prevent clinical reactions from occurring at an optimal rate that sustains life. In chemical reactions, a potential-energy barrier impedes a reaction therefore lowering the overall rate at which it can occur. The enzyme lowers this activation energy which serves as the said barrier of chemical reactions. Therefore, reactions depend on the catalyzing activity of enzymes to ‘speed up’ the reaction, this is vital in clinical settings. In a reaction catalyzed by an enzyme, the reacting molecules are called the substrate. The substrate molecules combine with the active site or epitope of the enzyme forming a temporary complex called the enzyme-substrate complex. This attachment of substrate to enzyme is known as the ‘lock and key’ mechanism in which the lock is the enzyme and the substrate is the key which ‘unlocks’ the enzyme through subsequent activation. The enzyme is not used in the reaction; rather it is re-formed as a product, and unchanged in structure. It can thus be repeatedly used as a catalyst in subsequent reactions. Because enzymes are proteins, they are prone to denaturation under ‘unfavorable’ conditions. The optimum level of enzyme functionality is the critical point – which occurs exactly before the point of denaturation. The intention of this experiment is to observe the enzymatic reaction of catechol oxidase, an enzyme that catalyzes the conversion of the catechol to a benzoquinone. Catechol naturally occurs in cells of various organisms. This reaction can be observed when the skin of a starchy fruit or vegetable (such as potato and apple) is injured and exposed to air. Consequently, the
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starchy interior of the fruit or vegetable will turn a brownish color. The source of catechol in this
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