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What is the time-course of enzyme to catalyze the breakdown of a protein, into its smaller units, amino acids?

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Research Question: What is the time-course of enzyme to catalyze the breakdown of a protein, into its smaller units, amino acids? Hypothesis: Adding an enzyme to the protein concentration will not only speed up the reaction but will also decrease the activation energy. The enzyme will have a fast rate of reaction initially and then will gradually start reaching a stop, when there is no more protein to be broken down, in which case the biuret solution will not change colour. Figure 1 : Lock and Key Theory1 Here is one of the proposed theories of how enzymes catalyze reactions, lock and key theory, suggests that the substrate (Albumin) will bind to an active site in the enzyme. The enzyme (Protease) will then hydrolyse the peptide bonds (Hydrogen bonds) and the product will be 2 amino acids. Using protein solutions at different concentrations (1%, 0.8%, 0.6%, 0.4%, 0.2% and 0%), and a mixture of biuret, I will calibrate the colorimeter. ...read more.


�10 Reliable Mean Albumin Concentration (%) 0 0,360 4 0,342 8 0,340 12 0,338 16 0,337 20 0,312 24 0,334 28 0,310 The rate of reaction seems to increase in the beginning (even though it is not very clear) and is it proceeds the reaction slow down. If the 20 and 25 seconds are excluded, then it is possible to see that to the end of the reaction the line is already reaching zero rate of reaction. Initial rate of reaction is faster than the rate of reaction at the middle or at the end, this is because as the reaction proceeds the Albumin will become more dilute and reach a point where there is no more Albumin for the Protease to catalyse, thus the limiting reactant of this reaction being Albumin. Conclusion: The results establish that the hypothesis is accurate (even though the results are not very accurate); the curve is steep at the beginning but then starts to level out in general. ...read more.


However this maybe misleading, because other particles are also present in the solution tricking the machine into believing that there is less light going through the solution, thus increasing the value of the colour (which then translates to the concentration of the solution). An even better idea to increase the accuracy of the results would be to increase the percentage of concentration present, for example increase the concentration to 5%, 10%, 15%, 20% etc... This would allow for overall accuracy increase and the anomalies would be spotted with more facility. A smaller limitation of this experiment is the fact that only one protein and enzyme was used, therefore the conclusion is only based on the results obtained. To improve this factor it would be effective to take several different proteins and enzymes; then it is possible to analyse the effect that enzymes have of the time course of the protein break down into amino acids. 1 http://www.tutorvista.com/biology/lock-and-key-hypothesis 2 http://wwwchem.csustan.edu/chem1112/DyeKinetics.htm 3 http://en.wikipedia.org/wiki/File:Michaelis-Menten_saturation_curve_of_an_enzyme_reaction.svg ?? ?? ?? ?? Biology Lab Report Raj Devraj ...read more.

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