BIOL 2051
June 10th 2013
Introduction
Enzymes are the ultimate catalysts of living things. Enzymes are made of proteins which are structured and directed by amino acids chains. Enzymes attract and fit substrate molecules to an active site. The active site binds the substrate molecules covalently to enzyme forming an enzyme-substrate complex, which catalyzes the substrate molecule into a product. Enzymes have the capability to break or build compounds which keep cell systems functioning. For example, our digestive tract has catabolic enzymes which break apart food for storage and reuse. Our lab experiment studied the relationship of benzoquinone production when altering the pH and temperature of the reaction, as well as enzyme and substrate concentrations. We used a Spec 20 to evaluate absorbance at 540 nm. Absorbance represents rate of product formation. We tested the substrate catechol and the enzyme catacholase and recorded the product benzoquinone. The objective was to identify the optimal conditions for the enzyme catacholase.
I predicted that the reaction rate will rise with increasing enzyme concentrations until an optimal reaction rate is attained. This is because there are only so many substrates that need to react with the active sites on the enzymes. Once this equilibrium is reached the graph will stabilize and remain constant.
I predicted that the reaction rate will increase with increasing substrate concentrations until an optimal point where there aren’t enough active sites on the enzymes to accommodate the influx of substrate molecules. At this point the graph will reach equilibrium and remain constant.
I predicted that heat would accelerate the reaction because if molecules have high kinetic energy their motions will become increasingly rapid. An incline in the graph will be evident but a