Lab Report Enzyme And Tyrosinase
Introduction: The purpose of this lab was to measure the extent of enzyme reaction on given substrates by means of color change. The reaction followed is given below: Tyrosinase³ Enzyme Pyrocatechol Hydroxyquinone Oxidation/Reduction Pink ³ Brown
E+S + [ES] = E+P Enzyme Reaction
Hypothesis: If there is an increase in enzyme concentration, an increase in reaction temperature, or an increase in buffer pH, then greater intensity in a given reaction will be experienced, resulting in greater manipulation of the final substrate product; measured by the extent of substrate color change. Greater manipulation of substrate when introduced into stronger, less diluted enzyme, …show more content…
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 ¡§Stock¡¨ enzyme with no dilution due to reaching a saturation point at which the enzyme reached its full catalytic potential.
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 enzyme¡¦s ability to act as a catalyst and hence decreased the rate and completeness of the reaction.
Graph Three …show more content…
Results show: as the buffer pH deviates from a neutral pH of 7.0, 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 bioavailability 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 enzyme¡¦s ability to act at its full potential as a catalyst. Reactions seemingly best occur when all conditions are ¡§neutral¡¨ (i.e. buffer pH =7.0 and temperature around room temperature +-28¢XC), and enzyme is completely pure and non-diluted (referred to as ¡§Stock
E+S + [ES] = E+P Enzyme Reaction
Hypothesis: If there is an increase in enzyme concentration, an increase in reaction temperature, or an increase in buffer pH, then greater intensity in a given reaction will be experienced, resulting in greater manipulation of the final substrate product; measured by the extent of substrate color change. Greater manipulation of substrate when introduced into stronger, less diluted enzyme, …show more content…
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 ¡§Stock¡¨ enzyme with no dilution due to reaching a saturation point at which the enzyme reached its full catalytic potential.
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 enzyme¡¦s ability to act as a catalyst and hence decreased the rate and completeness of the reaction.
Graph Three …show more content…
Results show: as the buffer pH deviates from a neutral pH of 7.0, 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 bioavailability 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 enzyme¡¦s ability to act at its full potential as a catalyst. Reactions seemingly best occur when all conditions are ¡§neutral¡¨ (i.e. buffer pH =7.0 and temperature around room temperature +-28¢XC), and enzyme is completely pure and non-diluted (referred to as ¡§Stock