AP Investigation Lab #13 Enzyme Activity
Background Information
Part 1 In the first part of the enzyme lab, we mixed a substrate and an indicator with an enzyme. There was also a neutral buffer in each of the chemical mixtures. The neutral buffer regulated the pH to around 7. We got a color palette and once we mixed each together, we observed and saw a change in the color of the substance. The darker and more brown the substance got, the more oxygen produced by the reaction. Our results showed that amount of oxygen produced increased about 10% a minute until it sort of equilibrated at 4 minutes and didn’t change to the fifth minute mark. If we were to change anything we did in the experiment, we would make our comparisons to the chart more precise. Overall we thought it was successful.
Part 2 In part two of the enzyme lab, we have 12 different test tubes, six of each (#1, 2, 4, 9, 11, and 12) being a substrate with guiacol product indicator, and a neutral buffer. The guiacol is a naturally organic compound and is actually a phosphate. The other six test tubes (#3, 5, 6, 7, 8, and 10) had the enzyme turnip peroxidase and different pH solutions for each of the six test tubes. The different pH levels were 3, 5, 6, 7, 8, and 10. The lower the pH, the more acidic the liquid is. The higher the pH, the more basic with alkaline. We mixed the six test tubes with the first tube of chemicals with their corresponding tube and pH as labeled in the instructions. We measured the rate of oxygen produced in each using the color palette like we did in part one of this lab. We found that the more neutral (closer to pH 7) the higher the reaction rate. When the pH level was very acidic or basic, the rate of reaction was lower. In terms of comparison to color, the more neutral the pH, the darker the solution was. The solution was lighter when the rate was lower. This happened because of the enzyme’s tolerance to outside factors. In this experiment, it was pH, but other factors could be temperature and the amount of
Part 1 In the first part of the enzyme lab, we mixed a substrate and an indicator with an enzyme. There was also a neutral buffer in each of the chemical mixtures. The neutral buffer regulated the pH to around 7. We got a color palette and once we mixed each together, we observed and saw a change in the color of the substance. The darker and more brown the substance got, the more oxygen produced by the reaction. Our results showed that amount of oxygen produced increased about 10% a minute until it sort of equilibrated at 4 minutes and didn’t change to the fifth minute mark. If we were to change anything we did in the experiment, we would make our comparisons to the chart more precise. Overall we thought it was successful.
Part 2 In part two of the enzyme lab, we have 12 different test tubes, six of each (#1, 2, 4, 9, 11, and 12) being a substrate with guiacol product indicator, and a neutral buffer. The guiacol is a naturally organic compound and is actually a phosphate. The other six test tubes (#3, 5, 6, 7, 8, and 10) had the enzyme turnip peroxidase and different pH solutions for each of the six test tubes. The different pH levels were 3, 5, 6, 7, 8, and 10. The lower the pH, the more acidic the liquid is. The higher the pH, the more basic with alkaline. We mixed the six test tubes with the first tube of chemicals with their corresponding tube and pH as labeled in the instructions. We measured the rate of oxygen produced in each using the color palette like we did in part one of this lab. We found that the more neutral (closer to pH 7) the higher the reaction rate. When the pH level was very acidic or basic, the rate of reaction was lower. In terms of comparison to color, the more neutral the pH, the darker the solution was. The solution was lighter when the rate was lower. This happened because of the enzyme’s tolerance to outside factors. In this experiment, it was pH, but other factors could be temperature and the amount of