Factors That Affect The Rate Of A Catalysis Reaction Essay

Factors That Affect The Rate Of A Catalysis Reaction Essay

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Through the results of this experiment, some of the factors that effect the rate of a catalysis reaction were able to be explored. As hypothesized, the 6 mL of distilled water did not catalyze with the catalase enzyme because it was not an appropriate substrate and does not produce any products with catalase. This result can be referenced to the lock and key model suggested by Emil Fischer explaining that the enzyme and substrate possess specific complementary geometric properties that would allow the substrate to fit into the active site of the enzyme like a key. Also, the water molecules did not act as appropriate substrates because of the enzymes lack of ability to break down H-O bonds in water and instead affect the peroxide bonds.
The 1.5% hydrogen peroxide concentration reaches a Vmax point of approximately 175 kPa which is also known as its saturation cap, whereas the 3% hydrogen peroxide concentration does not reach a Vmax point as it can be further extrapolated that the rate of reaction will continue to increase linearly past 5 minutes due to its non-hyperbolic relationship within the first 5 minutes. Evidently, as the amount of enzymes remain constant but the number of substrates are increased, the amount of products that are formed will increase initially - since the amount of collisions are increased - but reach a point where there are too many substrates and not enough enzymes, thereby stabilizing a constant speed of reaction until substrate levels are lowered. The enzymes are unaffected by an addition in substrate concentration as their protein structures are not compromised nor encounter any cause for denature.
The 3% hydrogen peroxide concentration’s rate of reaction kept on increasing and did not reach ...


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...thesized that the 3 mL distilled water and 3 mL hydrogen peroxide solution would display a stationary relationship which proved to be incorrect because it acted in the same way as the 1.5% concentration in Part B. Furthermore, it was predicted that the copper (II) sulphate and lead (II) nitrate added solutions will have similar slopes after they reach 1/2 Vmaz because they both inhibit the rate of enzyme activity within the solution non-competitively. This hypothesized proved to be somewhat true based on the results from the data. Copper (II) sulphate and lead (II) nitrate behaved similarly but they did not exhibit drastic or significant slopes before the 1/2 Vmaz point. This is due to the immediate effects that altered the sulphur-sulphur cross-bridges and breaking the peptide bonds in the tertiary structure of the enzyme - rendering it ineffective for catalysis.

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