LAB 1: What temperature does the enzyme actually work properly in? (Hypothesis) If the temperature is below 40 but above 20‚ then the liver will show bubbles. If the temperature is raised higher than the optimum temperature‚ then an extreme decline in enzyme activity would occur following by the quick denaturing of the enzyme‚ rendering it is permanently useless. Also about 37°C is body temperature. The liver that was at 25°C had a huge amount of bubbles (a 4 on the scale) and the 0°C
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environmental factors that effected the rate of enzyme reactions were the enzyme concentration‚ pH‚ and temperature. These environmental factors help enzymes break down the poisonous chemicals into harmless substance. When we tested the liver with 2ml of hydrogen peroxide for a normal reaction it showed that it was exothermic. We added more hydrogen peroxide and the reaction rate of the liver was 3. We learned that the catalase is reusable because the liver reacted both times when we put in the hydrogen
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Enzymes Reactions to Changes in Substrate and Inhibitors Benjamin J. Mora Coronado University of Texas Rio Grande Valley at Edinburgh Abstract Purpose for the experiments was to test the enzymes in various scenarios and see how changing this would affect the rate of reaction. The enzyme source used in the experiments was Turnip Extract. Concentrations of Turnip extract for activity 1 where o.5ml‚ 1.0ml‚ and 2.0 ml as for the rest of the activities 2 Through 4 stayed at a consistent concentration
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Lab report April 14‚ 2013 Abstract: In this article‚ we will experiment on the significant in strength of the enzyme by using three different test tubes and measuring the amount of product they give off. To determine this we are going to test the amount of color absorbance by using a special tool to help us understand our results. We will see how our end results show the effect of the amount of concentration we apply to each test tube. The results would be shown by the support of two graphs
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of the reaction: The effect of the temperature of the reaction on the activity of the purified enzyme was carried out by make the enzymatic reaction for 10 minutes at different temperature 25‚30‚35‚40‚45‚50‚60 and 70°C using an enzyme protein 0.1mg/reaction mixture and substrate concentration of 15 mg/reaction mixture‚ using a control of previously heated enzyme solution in the reaction. The data recorded in (table 27) and (figure 29) illustrate the effect of temperature of the reaction on the pectinase
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Enzyme Lab 6 03/13/2013 Report by Mary Jo Anthony I. Introduction II. Materials and Methods III. Results IV. Conclusion and Discussion Introduction Background Information: This lab allowed us to study chemical reactions and how catalysts will affect the rate of these reactions. The reaction we studied is the breakdown of hydrogen peroxide to water and oxygen and it is vital to life. The molecule hydrogen peroxide is a molecule that is toxic
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Enzyme Lab Introduction/ Abstract An enzyme is a substance produced by a living organism that acts as a catalyst to bring about a specific biochemical reaction. They are mainly made up of proteins and can tremendously speed up reactions. E. coli ( a bacterium) has about 1‚000 different types of enzymes floating around in its cytoplasm at any given time. Enzymes can be used to join and even break up molecules as shown in the diagram below. (1)
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environments affecting the rate of reaction‚ PNPP (p-nitrophenyl phosphate) + H20 ? PNP (p-nitrophenol) + H3P04. This reaction is catalyzed by the enzyme phosphatase. Different environments produced different reaction rates as environmental factors affect the efficiency of phosphatase. This is because environmental factors can change the tertiary structure of phosphatase‚ which alters its active site‚ and thus changes its efficiency to catalyze the reaction. We measured the rate of reaction‚ by using a chromogenic
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The effect of time on enzyme reaction. Abstract: In this lab investigation we will observe how the amount of hydrogen peroxide is affected by catalase over time. The enzyme was added to 10 mL’s of hydrogen peroxide and observed over time to determine the relation between time and enzyme activity. The hypothesis stated that as time increased substrate would decrease. Therefore I predicted that at 60 seconds‚ there would be the least amount of H2O2. The enzyme activity mirrored my predictions
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Inhibitory and Non-Inhibitory Competition‚ Enzyme-Substrate Concentration‚ Along with Varying Temperature and pH-Balanced Environments on the Enzyme-Catalyzed Reaction of pNPP Abstract: Introduction: Many of the chemical reactions‚ which take place in in living things are controlled by enzymes. In such cases‚ the enzyme is a protein in the cell which lowers the activation energy of a catalyzed reaction‚ which serves to increase the rate of the reaction. Alkaline phosphatase is made throughout
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