Catalase Lab Report

Nevertheless, the effects caused by the breakage of bonds will eventually lead to a decrease in the rate of reaction. As seen in the data, the reaction rate increased from 0.088 to 0.101 throughout the interval of -5℃ to 20℃ then decreased to 0.037 throughout the interval 20℃ to 56℃. This can be explained by the fact that 20℃ is the optimal temperature, therefore the active site of the enzyme is complementary to the substrate, causing the rate of reaction to be

Abstract In this experiment it was examined whether the enzyme peroxidase will work fastest in a pH of 8.0. We placed the enzyme peroxidase in a reaction with guaiacol and hydrogen peroxide in four different pH solutions. Then recorded the absorbencies for each reaction until all substrates were used up, and calculated the initial reaction velocities for each. We found that the reaction in a pH 7.0 solution had the highest initial reaction velocity.

7. Will the temperature effect the pH Scale? Hypothesis: The hypothesis of this experiment is that the rate of reaction will increases well as the hydrogen peroxide concentration. If the temperature, pH and enzyme concentration is kept constant then the rate of reaction will start to decrease as well as the hydrogen peroxide concentration. Aim: To investigate the effects of changing the concentration of the enzyme catalase that it has on the rate of breaking down the Hydrogen Peroxide solution.

After record your data and determine the absolute rate of the enzyme-catalyzed reaction. Based on the data and observations the hypothesis was accepted. It was accepted because when pH were changed to a variety of levels the transmittance began to get higher reaction rates. The increased absorbance means greater amount of product and a higher reaction rate will be produced.

It was expected that an extreme temperature would decrease the rate of reaction and results observed support that idea. With reference to figure 1, the peak performance of catalase was at 30℃, which was the closest to its usual environment

It was hypothesized that the optimal pH for the enzyme was pH 7 while the 1.0 ml peroxidase would have the best reaction rate. At the end of the experiment the results prove the hypothesis to be incorrect. INTRODUCTION Enzymes are proteins that allow a reaction to speed up. These proteins are made up of monomers known as amino acids.

The purpose of this study is to investigate the effects of varying the concentration of peroxidase on rate of reaction, as well as, the varying temperature and pH levels. Enzymes are proteins that catalyze biochemical reactions that work by reducing the activation energy for each reaction, causing an increase to the rate of the reaction. One class of enzymes are known as peroxidase. Peroxidase catalyze the oxidation of a particular substrate by hydrogen peroxide. Meaning that it eliminates H2O2 in order to prevent damage to the cells and tissues (Department of Biology University of Tampa 74).

The effect of pH on the speed of enzyme interaction with substrate chemicals Hypothesis: About pH: If the pH level is less than 5, then the speed of the enzyme reaction will be slower. About temperature: If the temperature stays the same, then the speed of the enzyme reaction will not be completely affected. Background information: The function of enzymes is to speed up the biochemical reaction by lowering the activation energy, they do this by colliding with the substrate.

LABORATORY REPORT Activity: Enzyme Activity Name: Natalie Banc Instructor: Elizabeth Kraske Date: 09.26.2016 Predictions 1. Sucrase will have the greatest activity at pH 6 2. Sucrase will have the greatest activity at 50 °C (122 °F) 3.

For example, between pH 5 and 7, there is an almost 500 mL difference, even though they are only 2.0 away on the pH scale. This shows even small changes in pH can have a large difference in the rate of reaction. Evaluation of Conclusion: The data and conclusion does match with previous background research. Background research suggests that reaction rate increases with pH until a point where optimum pH is reached, after which the enzyme is denatured and no longer can perform its function. This research was also shown in the data, even though the point at which the enzyme denatured was not

LABORATORY REPORT Activity: Enzyme Activity Name: Natalie Banc Instructor: Elizabeth Kraske Date: 09.22.2016 Predictions 1. Sucrase will have the greatest activity at pH 6 2. Sucrase will have the greatest activity at 50 °C (122 °F) 3. Sucrase activity increases with increasing sucrose concentration Materials and Methods Effect of pH on Enzyme Activity 1. Dependent Variable amount of product (glucose and fructose) produced 2.

Introduction 1.1 Aim: To determine the kinetic parameters, Vmax and Km, of the alkaline phosphatase enzyme through the determination of the optimum pH and temperature. 1.2 Theory and Principles (General Background): Enzymes are highly specific protein catalysts that are utilised in chemical reactions in biological systems.1 Enzymes, being catalysts, decrease the activation energy required to convert substrates to products. They do this by attaching to the substrate to form an intermediate; the substrate binds to the active site of the enzyme. Then, another or the same enzyme reacts with the intermediate to form the final product.2 The rate of enzyme-catalysed reactions is influenced by different environmental conditions, such as: concentration

Based on the results from Part A, the enzyme concentration is directly proportional to the rate of reaction. This means that as enzyme concentration increases so does that rate of reaction when the catalase is placed in the 140ml of 3% hydrogen peroxide. Referring back to Graph 1.1 it is evident that the there is a steady increase in rate of reaction as the concentration went up which explains why the line of best fit is positive. This relation happens because the substrate concentration of the 3% hydrogen peroxide is always in excess in comparison to the enzyme catalase concentration then as we increase the concentration of catalase there will always be a substrate that may be catalyzed. Factors that may affect this relationship would be temperature

ABSTRACT: The purpose of the experiments for week 5 and week 6 support each other in the further understanding of enzyme reactions. During week 5, the effects of a substrate and enzyme concentration on enzyme reaction rate was observed. Week 6, the effects of temperature and inhibitor on a reaction rate were monitored. For testing the effects of concentrations, we needed to use the table that was used in week 3, Cells.

It was expected that the change in pH disrupts enzyme’s structure when its side chains containing -COOH and –NH2 gain or lose H+ ions (Anglin, M., September 2, 2014). The deformed active sites are incapable of binding the substrate and facilitating the reaction. Altering the pH of the solution altered the tertiary structure of the enzyme rennet by changing bonds between each side chains on the amino acid. Some amino acid side chains have ionic charges and use ionic bonds in order to create tertiary structures (Clark, J., 2007). Modifying the pH of milk originally at 6.5 to 5, 7, 8 and 9 changed the charges on the ionic side chains.