Enzymes Lab Report Revised Sample

Enzymes Lab Report Revised Paper Activation energy is the lowest amount of energy needed to begin a chemical reaction (Campbell and Erect, 2008). Few biochemical reactions could take place quickly enough to satisfy the metabolic needs for living organisms without the aid of enzymes (Helms et al. , 1998). Biological enzymes used in cells are seen in the form of proteins. These catalysts have complex structures including one or more polypeptide chains which are folded in specific shapes to contain an active site, which is the area a substrate will bind to the enzyme. A substrate is a molecule which the enzyme will act upon and change (Helms et al. 1998). The substrate which is bonded to its specific enzyme is known as an enzyme-substrate complex, and the results of the Atlantic action between the enzyme and substrate change the substrate to the product(s) of the reaction (Campbell and Erect, 2008). The active site of an enzyme is specific for the substrate. According to Campbell and Erect, when the substrate enters th e active site the shape of the enzyme will change very minutely to better fit the substrate in the active site. The very tight fit between the substrate and the active site is called an induced fit (Campbell and Erect, 2008). This induced fit or conformational change is another reason why the activation energy is lowered during the chemical reaction (Garcia-Viola et al. , 004). The enzyme that is being tested throughout this experiment is the enzyme catecholamine. According to Helms et al. , catecholamine is found in a few fruits and vegetables and is responsible for the inside of the fruit or vegetable turning brown when exposed to air. The brown color is a result of the cathode oxidation and conversion to Benzedrine. The Benzedrine forms chains that are the structural centerpieces of the brown and red pigments that cause the fruit to darken. We will write a custom essay sample on Enzymes Lab Report Revised specifically for you for only $16.38 $13.9/page Order now We will write a custom essay sample on Enzymes Lab Report Revised specifically for you FOR ONLY $16.38 $13.9/page Hire Writer We will write a custom essay sample on Enzymes Lab Report Revised specifically for you FOR ONLY $16.38 $13.9/page Hire Writer The activity of catecholamine is based on some environmental factors (Helms et al. , 1998). The purpose of this experiment is to test some of these environmental factors such as temperature, pH, enzyme concentration, and substrate concentration in order to find out what effects each have on the efficiency and productivity of the enzyme. Hypotheses Temperature The null hypothesis is that the temperature of the system will have no effect on the enzymatic activity. The alternative hypothesis is that an increase in the temperature of the system will increase the amount of enzymatic activity. H The null hypothesis is the pH of solution will have no effect on the enzymatic activity. The alternative hypothesis is the enzyme used will have an ideal PH. A solution with too high or too low pH will cause a decrease in the amount of enzymatic activity observed. Enzyme Concentration The null hypothesis is enzyme concentration will have no effect on the enzymatic activity. The alternative hypothes is is an increase in enzyme concentration will increase the enzymatic activity. The converse will also be true. Substrate Concentration The null hypothesis is the substrate concentration will have no effect on the enzymatic activity. The alternative hypothesis is an increase in substrate concentration will increase the amount of enzymatic activity. Materials and Methods: To test the effect of temperature, three test tubes were labeled 10, 24, 50, and filled with 3 ml of a phosphate buffer of pH 7. One test tube was placed in an ice bath, one was left at room temperature, and the final test tube was placed in a heated beaker of water. The three solutions were allowed to sit for ten minutes, in order to allow the chilled test tube to reach ICC and the heated solution to reach at least ICC. Two new test tubes were then filled with potato juice, and two more were filled with Cathode. One of each of these solutions was placed in the ice bath and the heated beaker respectively. After ten more minutes, ten drops of cathode was added to each of the tubes containing the buffer solution of pH 7. Room temperature cathode was then added to tube 24, the chilled cathode was added to tube 10, and the heated cathode was added to tube 50. Ten drops of potato juice was then added to each of the test tubes. The test tubes were then allowed to stand for five minutes with each mixture being shaken every two minutes. The mixtures were then observed and the intensity of the color of each solution was recorded. PH In order to test the effects of pH level on enzyme activity, seven test tubes babbled pH 4, pH 5, pH 6, pH 7, pH 8, pH 9, and pH 10 were filled with 3 ml of a buffer of the same PH. Ten drops of cathode was then added to each solution. The test tubes were covered with Paraffin, and then inverted several times. The solutions were allowed to stand five minutes, being mixed each minute. The solutions were then observed and the intensity of the color of each solution was recorded. Enzyme Concentration In order to examine the effects of enzyme concentration on the cavity of the enzyme, first, four test tubes were labeled A, B, C, and D respectively. These test tubes were filled in alphabetical order using a pipette with 3 ml plus 20 drops, 3 ml plus 15 drops, 3 ml plus 10 drops, and 3 ml of pH 7 phosphate buffer. In addition, O, 5, 10, and 20 drops of potato juice were added to the test tubes respectively. Following the addition of these substances, 10 drops of cathode was placed in each test tube, and then covered with Paraffin. Each test tube was inverted 4-5 times, and allowed to stand for 3-4 minutes while mixing the contents of each tube once every minute. The reaction in each tube was observed and the color intensity in each was recorded. Substrate Concentration In order to test the effects of substrate concentration on enzyme activity, eight test tubes labeled 1, 2, 4, 8, 16, 24, 32, and 48 were filled with 5 ml of a phosphate buffer of pH 7. Each tube had additional 47, 46, 44, 40, 32, 24, and 16 drops (one tube had no additional drops respectively. Each tube had drops of cathode added with respect to the numbered label (test tube 1 had 1 drop of cathode, test tube 16 had 16 drops, etc. ). After these solutions were mixed, each tube was covered with Paraffin and inverted 3-4 times. The film was removed from the tubes and 30 drops of diluted potato juice was added to each, covered tit Paraffin again, inverted 3-4 times, and allowed to sit at room temperature uncovered. The tubes were observed and the intensity of the colors in each tube was recorded. Results: Tablet: Effect of Temperature on Enzyme Activity Effect of Temperature on Enzyme Activity Test Tube Temp. F Solution Color intensity 10 ICC 24 ICC 50 520 c In table 1, the effect of temperature on enzyme activity is shown. Attic, test tube 10 showed medium color intensity. At ICC, test tube 24 showed a high level of color intensity. At 520 C, test tube 50 showed the lowest level of color intensity. Tablet: The effect of pH levels on enzyme activity in solution. In this case, the addition of+ indicates a more intense color. Effect of pH on Enzyme Activity pH of Solution Color Intensity 4 5 6 7 8 9 In table 2, the effect of pH on the enzymatic activity in solution is shown. As pH rose for the solution, the color intensity rose as well, until a pH of 8 was reached. In between pH of 8 and pH of 9, the color intensity dramatically dropped. At pH of 10, no color was recorded for the solution. Table 3: The effect of enzyme concentration on enzyme activity based on the intensity of the color of solution. In this case, the addition of + indicates a more intense color. Intensity of Color in Different Enzymatic Concentrations Brown/Yellow + Brown ++ Red/Brown +++ In table 3, the intensity of color in different enzymatic concentrations is shown. In test tube A, which contained no enzyme, no color was recorded. As the concentrations of enzyme in solution increased in the sequential test tubes (B, C, and D respectively), the color intensity also increased from a light brown/yellow color, to a dark reddish/brown color. Table 4: A qualitative observation of the effect of substrate concentration on enzyme activity Effect of Substrate Concentration on Enzyme Activity Amount Buffer (ml) Amount Cathode (drops) 5 + 47 drops 2 5+46 drops 5+44 drops 5 + 40 drops 16 5 + 32 drops 5 + 24 drops 32 5+ 10 drops 5+ 0 drops 48 In table 4, the effect of the substrate concentration in solution on the enzymatic activity is shown. In test tube 1, a very limited amount of substrate was added, which showed no change in color. In the sequential test tubes, color intensity gradually rose as the concentration of substrate increased from two drops to forty-eight drops. Discussion: In this study, the optimal temperature for catecholamine was found to be ICC. If the temperature is lower or higher than the enzymes optimal temperature, the productivity of the enzyme will decrease (Helms et al. , 1998). At a certain point in temperature increase, the protein becomes denatured (Campbell and Reese, 2008). In this study, the alternative hypothesis stating an increase in the temperature of the system will increase the amount of enzymatic activity was accepted. The rapid motion of the substrate molecules running into the enzyme molecules more often at higher temperatures may be the reason why increasing temperature is effective (Campbell and Erect, 2008). The breaking down of the secondary and tertiary protein structure of the enzyme are different forms of demutualization. The temperature being too low results in the enzymatic reaction being slower as well (Campbell and Erect, 2008). H Catecholamine was found to have the greatest amount of activity in solution of pH eight. If the solution an enzyme is in becomes too basic or acidic than the enzymes optimal pH, it will be less productive and the secondary and tertiary structure of the protein will be denatured (Helms et al. , 1998). The alternative hypothesis is the enzyme used will have an ideal PH. The study shows that a solution with t oo high or too low pH will cause a decrease in the amount of enzymatic activity observed. The alternative hypothesis was accepted by this portion of the study as well. A solution with too high or too low pH will cause a decrease in the amount of enzymatic activity observed. Most enzymes prefer an optimum pH between 6 and 8 (Campbell and Erect, 2008). This suggests each enzyme adapts to its environment for the best results possible (Campbell and Erect, 2008). Enzyme Concentration Increasing the amount of enzyme present increases the rate at which the action is taking place (Helms et al. , 1998). The increased concentration of enzyme in solution also caused the productivity of catecholamine to have increased until there was not enough substrate to bind with the catecholamine enzyme. The experiment showed that the most concentrated solution with enzyme produced the most intense color change. Thus, the alternative hypothesis stating that an increase in enzyme concentration will increase the enzymatic activity was accepted by the experiment. Substrate Concentration At a certain point when there is not enough substrate, the enzymes will not aka the reaction go faster. If you instead increase the amount of substrate present, the reaction speed will also increase (Helms et al. , 1998). The increased amount of substrate present caused the enzyme to be more productive as well. This occurred until the catecholamine reached its maximum efficiency and the solution became saturated with substrate. At this point, the increased productivity plateau and leveled off. The maximum efficiency of the enzyme was determined to be when 16 drops of cathode were put into test tube number 16. Once again, the alternative hypothesis was accepted by this experiment, which showed an increase in substrate concentration will increase the amount of enzymatic activity. This study is beneficial due to the vast number of enzymes that are required for life.