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Greater manipulation of substrate when introduced into stronger, less diluted enzyme, higher buffer pH, and/or higher temperature is expected. We know that color change is an effective method of measuring chemical activity within a given reaction. The stronger, more drastic the color change, the more chemical activity present. For this experiment we are concerned with enzyme activity. Knowing that enzymes act as catalysts within a chemical reaction, the extent of color change present should shed light into the character of the given enzyme. Results:
Experiment One: As enzyme concentration increases, color change from pink to brown increases. Therefore, we know that the rate and the extent of the reaction increases, (as measured by color change) due to greater enzyme activity. Graph One Explains: Experiment Two: As enzyme concentration increases, an increase in color change is seen. However, there appeared a saturation point. Color change did not increase from 1:1 ratio of dilution to sticks” enzyme with no dilution due to reaching a saturation point at which the enzyme reached its full catalytic attention.
Graph Two Explains: Experiment Three: As deviation from a neutral pH of 7. 0 within the buffer is presented, the rate and completion of the given reaction was hindered. Greatest color change, hence greatest enzyme activity is seen at a neutral pH of 7. 0, concerning the buffer solution. Increase and decrease in pH within the buffer seems to put strain on the enzymes : s ability to act as a catalyst and hence decreased the rate and completeness of the reaction.
Graph Three Explains: Experiment Four: As deviations from around room temperature (+- COX) re introduced to the reaction, the rate and completeness of the reaction is seemingly hindered. Cooling the reaction to around COX slowed the reaction. Heating the reaction to around 1 COX denatured the enzyme and no reaction occurred. Graph Four Explains: Conclusion and Discussion: Hypothesis was confirmed concerning the effect upon the reaction of enzyme concentration but refuted upon the effect of the pH of the buffer solution and refuted upon the effect of temperature on the reaction.
Results show: as the buffer pH deviates from a neutral pH of 7. , the reaction is slowed and/or inhibited; cooling or heating the reaction slows and/or inhibits the rate and/or completeness of the reaction. The availability of enzymes is hindered by deviating the temperature and/or the pH of the buffer solution; hence, the color change of the product is less drastic and intense, drastic being dark brown, somewhat reactive being pink, and non-reactive being colorless/clear; thus, chemical activity was hindered due to lack of the enzymes : s ability to act at its full potential as a catalyst.