Enzyme Activity
Enzyme Catalase Activity in Reaction with the Substrate Hydrogen Peroxide
Abstract
We performed these experiments to observe the effects of enzymes on the rate of reactions. We tested and compared the activity of the enzyme catalase on the substrate H2O2 in various states and percentages, and observed the absorption values of the enzyme-substrate relationship at different concentrations. Our results show that the more substrate available, the quicker the reaction will happen except in one test, which might mean that a balanced concentration of the two is most beneficial.
Introduction
The objectives of these experiments were to observe the effects of the enzyme-substrate relationships and to record our findings. Enzymes increase the rate of reactions by lowering the energy needed to activate the reaction (McNeil et al. 2013). Enzymes will work with substrates to produce reactions and products and they will bind together at an active site. They will only bond to with particular molecules and environmental factors can also affect their productivity. They are proteins, and proteins are made up of many amino acids (Brian et al. 2013). We used the enzyme catalase that occurs naturally in many organisms to study the qualitative and quantitative results of enzymatic activity. My hypothesis is that the findings in these experiments will show that the enzyme catalase will increase the rate of reaction with the substrate.
Methods
In Activity 1 Procedure A, we had four test tubes filled with different components. The table below shows each tube’s components. In each test tube, we added 5.0 mL 3% H2O2. We recorded initial observations and checked frequently for changes. Table 1. Tube # | Contents | 1 | 1 mL H2O | 2 | ¼ × ¼” potato cube | 3 | 1 mL Enz. | 4 | 1 mL Enz boiled for 5 minutes, then cooled |
In Activity 1 Procedure B, we prepared two more test tubes with different substrates. In each empty tube we put 1 mL of enzyme. To that, we added
Abstract
We performed these experiments to observe the effects of enzymes on the rate of reactions. We tested and compared the activity of the enzyme catalase on the substrate H2O2 in various states and percentages, and observed the absorption values of the enzyme-substrate relationship at different concentrations. Our results show that the more substrate available, the quicker the reaction will happen except in one test, which might mean that a balanced concentration of the two is most beneficial.
Introduction
The objectives of these experiments were to observe the effects of the enzyme-substrate relationships and to record our findings. Enzymes increase the rate of reactions by lowering the energy needed to activate the reaction (McNeil et al. 2013). Enzymes will work with substrates to produce reactions and products and they will bind together at an active site. They will only bond to with particular molecules and environmental factors can also affect their productivity. They are proteins, and proteins are made up of many amino acids (Brian et al. 2013). We used the enzyme catalase that occurs naturally in many organisms to study the qualitative and quantitative results of enzymatic activity. My hypothesis is that the findings in these experiments will show that the enzyme catalase will increase the rate of reaction with the substrate.
Methods
In Activity 1 Procedure A, we had four test tubes filled with different components. The table below shows each tube’s components. In each test tube, we added 5.0 mL 3% H2O2. We recorded initial observations and checked frequently for changes. Table 1. Tube # | Contents | 1 | 1 mL H2O | 2 | ¼ × ¼” potato cube | 3 | 1 mL Enz. | 4 | 1 mL Enz boiled for 5 minutes, then cooled |
In Activity 1 Procedure B, we prepared two more test tubes with different substrates. In each empty tube we put 1 mL of enzyme. To that, we added