10_19_07 lab_2

10_19_07 lab_2 - 1 Title: FACTORS INFLUENCING ENZYME...

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Title: FACTORS INFLUENCING ENZYME ACTIVITY (ENZYME CONCENTRATION, SUBSTRATE CONCENTRATION, PH LEVEL, TEMPERATURE RATE) OF ALKALINE PHOSPHATASE, SEMI-QUANTITATIVE ESTIMATES OF ENZYME ACTIVITY, AND EFFECTS ON ENZYME ACTIVITY BY NON COMPETITIVE AND COMPETITIVE INHIBITORS INCLUDING: POTASSIUM MOLYBDATE, POTASSIUM PHOSPHATE (INORGANIC PHOSPHATE), PHENYL PHOSPHONATE Abstract: Various experiments were performed to study the effects on reaction rates that inhibitory compounds, enzyme and substrate concentration, pH, and temperature had. Inhibitory compounds all slowed the reaction rate, with inorganic phosphate slowing it down the most. Increase in enzyme concentration was directly proportional to increase in reaction rate. Increase in substrate concentration was directly proportional to increase in reaction rate in small amounts; as substrate concentration grew to higher levels, reaction rate leveled off . Enzymes function best at a pH optimum of 10.0 and temperature optimum of 37°C for the enzyme to produce the highest reaction rate. These findings suggest that all but the first factor increase reaction rates. Introduction: Enzymes are biological catalysts that decrease the activation energy of a reaction and thereby increase its speed without being consumed. The substance on which an enzyme acts is referred to as a substrate. Enzymes, in general, work best under certain narrowly defined parameters, such as appropriate temperature, pH, and ion concentration. Any departure from optimal conditions adversely affects enzyme activity ( Solomon et al. 2008 ). Competitive and noncompetitive inhibition also work against enzyme activity, whether by 1
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directly blocking the enzyme’s active site to which the substrate binds to (competitive inhibition) or by binding to the enzyme’s allosteric site and changing the shape of its active site, rendering substrate binding impossible (noncompetitive inhibition) ( Solomon et al. 2008 ). This study investigates how enzyme activity is quantitatively affected by the above factors, as well as varying levels of enzyme and substrate concentrations. One variable that will be tested is the effects of inhibitors on the rate of a reaction. The three inhibitors used in this study are: molybdate, potassium phosphate (inorganic phosphate), and phenyl phosphonate. It is predicted that each will slow the reaction rate. Molybdate will function as a non-competitive inhibitor, blocking the cofactor zinc from binding to the cofactor site. Potassium phosphate will shift the equilibrium of the reaction to the left, thereby slowing the rate of the reaction. Phenyl phosphonate will competitively inhibit by binding to the enzyme’s active site. Enzyme concentration is predicted to increase the reaction rate in direct proportion to
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10_19_07 lab_2 - 1 Title: FACTORS INFLUENCING ENZYME...

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