To determine the effect of enzyme concentration and substrate concentration on the reaction rate, we performed a serial elution of enzymes to get test tubes with full, one-half, one-fourth, and one- eighth concentrations. We then used a spectrophotometer to get the absorbency reading over time, and we used these readings to determine the reaction rate. We did the same thing with a serial dilution for substrate concentration, and we found the reaction rate for these as well. We found that as enzyme concentration decreased, the reaction rate decreased as well.
For example, the rate of the reaction at one-half enzyme concentration was 0. 95 while the rate of the reaction at one-eighth enzyme concentration was . 32. We also found that as substrate concentration decreased, the reaction rate also decreased. For example, the reaction rate at one-half substrate concentration was 0. 089, and the reaction rate at one- eighth substrate concentration was 0. 011. Overall, our results show that enzyme and substrate concentrations both have an impact on the rate of the reaction. INTRODUCTION All cells depend on chemical reactions in order to survive (Schultz 2006).
The amount of energy required to convert substrates to products in these chemical reactions is called the activation energy. Proteins called enzymes help to decrease the reaction rate of these chemical reactions by lowering the activation energy required. Reactions that require less activation energy will react at a quicker rate. The process by which enzymes bind to substrates is called the enzyme-substrate complex. Enzymes attach to substrates at the active-site, and this is where the reaction occurs. The enzyme then releases the newly formed products, and the enzyme is free to bond to more substrates; the process starts over again.
A spectrophotometer was used to measure the absorbency of reactions in est.. Tubes of different dilutions of enzyme concentration and substrate concentration. The absorbency readings were averaged over time, and this gave the reaction rates. The substrates of the reaction were cathode and oxygen(02), the enzyme was cathode oxides, and the products were water(H2O) and Roth- quinine. Potatoes contain an enzyme called cathode oxides. When this enzyme has access to oxygen and cathode it will react to produce Roth-quinine. It is a defensive response in potatoes, and it causes the potato to turn brown and stink.
This is done in order to avoid being consumed by other organisms. We hypothesized that as enzyme concentration increases, the reaction rate would increase as well. We also hypothesized that as substrate concentration increases, the reaction rate will also increase. The purpose of this experiment is to determine whether enzyme and concentration have an effect on the reaction rate. METHODS A potato was cut into small pieces, and placed into a blender with water. This substance was then placed into centrifuge tubes, and placed into a centrifuge at 2000 RPM for about 5 minutes in order to homogenate the potato.
This produced a pellet which was the solid part, and a supernatant which was the liquid part. The supernatant was the cathode oxides which would be the enzyme for the reaction. We made a dilution series of enzyme solution with full strength, one-half strength, one-fourth strength, and one-eighth strength concentrations. The original enzyme solution was pure cathode oxides which was obtained from the supernatant of the homogenates potato. The serial dilution was made by putting ml of the original solution into another test tube.
Three ml of water was added to this solution to reduce an enzyme solution at half strength; 3 ml of this solution was then put into another test tube, and 3 ml of water was added to this new solution to produce an enzyme solution at one-fourth strength. Three ml of the one-fourth strength enzyme solution was put into another test tube, and 3 ml of water was added to produce a one-eighth strength enzyme solution. We then added 1 ml of each of these solutions of enzymes to 5 ml of buffered cathode to start a chemical reaction and observed the effect of the concentration of enzyme on the reaction rate.
We placed the spec tubes intonating the solutions in a spectrophotometer one at a time to get the absorbency readings of each. We recorded the absorbency reading every minute for 3 minutes and used this data to calculate the reaction rates. We did a similar experiment to determine the effect of substrate concentration on reaction rate. We made another series of dilutions of 0. MM cathode with full strength, one-half strength, one-fourth strength, one-eighth strength, and one-sixteenth strength concentration. We added 1 ml of each of these solutions to a spec tube containing 3 ml of water and 1 ml of potassium phosphate buffer.
We then used the spectrophotometer to get the absorbency readings of each and used these readings to determine the reaction rates and how they are affected by substrate concentration.