Effect of Abiotic Factors on an Enzyme
Enzymes are biological catalysts; they cause reactions to happen that would not normally occur due to the activation energy that would be required - Effect of Abiotic Factors on an Enzyme introduction. They bring together substrates and cause chemical reactions that are essential for life. Without enzymes life processes, and life in of itself, would not be possible. Enzymes are also special because very little of the actual enzyme is actually used up in the reaction. In this lab two different factors, temperature and pH, were tested to see what type of effect they would have on catalase, a potato enzyme that synthesizes H2O2. The data my group collected supported one hypothesis, that an acidic environment would not be conductive to enzyme behavior, and disproved another, that higher temperatures would yield greater enzyme byproduct production.
Enzymes are biological catalysts and are necessary for life to occur. They bring together substrates and begin chemical reactions that would otherwise not happen due to the high amount of energy that they would require. Organisms are sensitive to their environments and must maintain homeostasis in order for their life processes to properly take place. This is due in part to the fact that enzymes can only function in certain pH and temperature levels specific to that enzyme. When levels rise or fall below these levels, it will affect the enzyme, and in turn the organism. At moderate level breaches the enzyme will not work properly, and at high level breaches the enzyme will break down, and the reaction will never occur. This could kill the organism that the enzyme belonged to. In this lab, the reaction of a potato enzyme, catalase, was measured by use of bubble height. The two abiotic factors that we were using to test the catalase were high-low temperatures and high-low pH systems. For the temperature experiment I hypothesized that the higher temperature would yield more enzyme activity, and therefore a taller bubble column due to there being more energy available in the system. For the pH experiment I hypothesized that the enzyme would not work in the low pH and work just as well as, if not better, in the high pH level system. This is because the acid would have denatured the enzyme, and broken it down, while the basic solution would have had little to no effect on the enzyme.
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Four test tubes were obtained, and an equal amount of the substrate, in this case H2O2, was obtained. One of the test tubes was submerged in an ice water bath, and kept there until its temperature reached 5˚C. Another test tube was placed into a hot water bath until its temperature reached 60˚C. The third test tube was augmented with a small amount of acetic acid, lowering its pH levels into the 2-3 zone. The last test tube had ammonia added to the substrate, raising its pH into the 9-10 range. Doing temperature first, semi-equal amounts of catalase were added into the heated or cooled substrate. This reaction was measured over the course of six minutes. For the pH experiments the same thing was done, but this time only measured for three minutes. Due to time restrictions. Results
For the heated enzyme-substrate mix, the amount of bubbles that did appear was significantly less than in the baseline experiment we did. After about a minute, the bubble column was no longer growing, and at two minutes the gas had completely dispersed.(see Fig. 1) For the cooled enzyme-substrate mix, the reaction was totally delayed, and happened over a much longer period of time. The reaction continued for twenty minutes, but was only actively measured for six. The bubbles reached their second highest point in this reaction (compare Fig. 1 to Fig. 2). In the acidic substrate-enzyme mix, nothing happened when the catalase was added into the mixture. And in the basic substrate-enzyme mix the reaction was quicker, and reached the highest point for bubble columns (compare Fig. 1 to Fig. 2). Discussion
I hypothesized that a heated environment would be more favorable for enzymatic reactions then a cold one. This was disproved through the course of the experiments that were conducted. It was instead proven that heated environments were unproductive for enzymes, and possibly denatured, or broke them down past usage point. It was evident when the heated reaction was far less efficient then its cooled counterpart (Table and Figure 1). This is because the high heat denatured, or broke down the enzyme before it could begin it’s processes. The cooled reaction on the other had was much more productive over all. (Fig. Table 1). The cooling of the substrate may have
slowed down the reaction over all, therefore allowing more bubbles to stay for longer, raising the overall height of the column. This is important because it states that enzymes can be effected by different temperatures in their environments, and can slow their processes or even stop them if they are unable to work in extreme conditions. The fact that the heat was so differential may have made a difference on why one reaction did what it did compared to the other I also hypothesized that enzymes in an acidic environment would have little, to no reaction, while that in a basic environment would react better. My hypothesis was proven, because the enzyme substrate mix in acid did nothing (Table 2). The enzyme-substrate mix in the base, however, worked much better than even the baseline data. This states that this particular enzyme works best in a more basic environment. With the acid, the enzyme was most likely broken down so completely that there was no opportunity for anything to even occur. When adding the acid and base, the amounts were not measured out exactly, and that could have made a big difference, seeing as one reaction could have had more or less acid or base to react with. These tests implicate that environmental factors can effect organisms down to the sub-cellular range. This also proves that enzymes have a range in which they are most effective. Works Cited
Hilker, J 2013 Investigation 13 Enzyme Activity