ipl-logo

Peroxidase Lab Report

1091 Words5 Pages

INTRODUCTION Substances that bind or react to each other use a certain amounts of energy to create a new product in a chemical reaction. Enzymes are proteins used in these reactions to create the same product using less of its supplied energy in that same amount of time. Enzymes are biocatalysts and will bind with the reactive molecules to create substrates forming enzyme-substrate complexes. These complex alter the chemical bonding in the molecules so that they react to each other in the same amount of time using less activation energy. There are certain factors that alter how effective an enzyme might be in the reaction. Enzymes function better in warmer temperatures, the heat causes the molecules to move faster which increases the likelihood …show more content…

We use peroxidase as our enzyme in the experiment. Peroxidase is found in plants, such as turnip, and can convert hydrogen peroxide to water and oxygen. We had which were hydrogen peroxide (3%) and hydroxylamine. The hydrogen peroxide competes with the hydroxylamine for the active site molecules from peroxidase. The peroxidase needs the hydrogen peroxide in order to separate it into water and oxygen. If enough of the hydroxylamine is used in the test tube, it will stop the enzyme from binding with the hydrogen peroxide causing competitive …show more content…

For accurate results on our experiment, we decided to break it up into three sections, testing only three test tubes at a time. We added all of our substances to our first three tubes right before we put them in the spectrophotometer and recorded their absorbency every 30 seconds for 5 minutes for each one. This gives us the most accurate results when testing for enzymes since we are giving each test tube the same amount of time for the chemicals to react to each other. We followed the same process for the two remaining sets of test

Show More
Related
881 Words | 4 Pages

Because of the fact that reactions are catalyzed by enzymes when they randomly collide with substrate molecules, increasing the temperature would increase the reaction rate. Increasing the temperature further increases the vibrational energy of the enzyme molecules, straining the bonds that keep them together. Furthermore, when the temperature is higher, more bonds will break because of these strains, causing the active site of the enzymes to change too. Similar to pH, a change in the shape of the active site leads to the substrate not being able to fit perfectly, leading to the enzyme not being able to catalyze the reaction. Overall, an increase in temperature will cause the rate of reaction to increase initially due to the increased kinetic energy.

Read More
1117 Words | 5 Pages

1 “substrate” and another “ enzyme.” Instead of using the distilled water, this time you are going to use different pH buffer in the enzyme test tube. In the substrate tube, add 7 mL of distilled water, 0.3 mL of hydrogen peroxide, and 0.2 mL of guaiacol for a total volume of 7.5 mL. For the enzyme tube, instead of distilled water add the pH solution (3) and 1.5 mL of peroxidase which equals a total volume of 7.5 mL. Use the dH2O syringe for our pH solution. To clean the syringe, flush it by drawing 6 mL of distilled water.

Read More
247 Words | 1 Pages

An enzyme can not be considered a reactant because, like catalysts, the enzyme is never used up in the reaction and is reused again in another chemical reaction. In this lab, the source of hydrogen peroxidase was the potato solution. The substrate that the hydrogen peroxidase acts upon is the hydrogen peroxide.

Read More
1090 Words | 5 Pages

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.

Read More
1407 Words | 6 Pages

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.

Read More
1764 Words | 8 Pages

Enzymes speed up chemical reactions enabling more products to be formed within a shorter span of time. Enzymes are fragile and easily disrupted by heat or other mild treatment. Studying the effect of temperature and substrate concentration on enzyme concentration allows better understanding of optimum conditions which enzymes can function. An example of an enzyme catalyzed reaction is enzymatic hydrolysis of an artificial substrate, o-Nitrophenylgalactoside (ONPG) used in place of lactose. Upon hydrolysis by B-galactosidase, a yellow colored compound o-Nitrophenol (ONP) is formed.

Read More
1138 Words | 5 Pages

Abstract: Peroxidase is an enzyme that is found in turnips that reacts with hydrogen peroxide. When guaiacol is introduced the reaction turns brown allowing the reaction to be measured through a spectrometer. In this lab the concentration of the enzyme is investigated producing the result that when the concentration is increased so does the rate of the reaction. When boiled in this experiment, the enzymes rate of reaction increases. The rate of reaction in enzymes is dependent on the concentration and temperature.

Read More
1381 Words | 6 Pages

We hypothesized that hydroxylamine was a competitive inhibitor that competes with the substrate for the active site. This was due to the fact that it has a similar structure to hydrogen peroxide, which means that it could fit into the enzyme active site, preventing the substrate from binding. The lab results were as expected since as soon as the inhibitor was introduced to the baseline enzyme catalyzed reaction, the absorbance value decreased from 0.254 to 0.017 as shown in Figure 6. In addition, our results show that the absorbance value of the inhibitor baseline reaction increased from 0.017 to 0.038 as the substrate concentration was doubled. This led us to the conclusion that hydroxylamine is a competitive inhibitor and not a noncompetitive inhibitor.

Read More
733 Words | 3 Pages

Abstract To figure out how temperature effects the change in the rate of an enzyme, test tubes were filled with solutions of buffer with a pH of 5, peroxidase, H2O2, and guaiacol and placed different water baths of the following temperatures: 4°C, room temperature (23°C), 32°C, and 60°C. To help determine the rate of reaction of peroxidase, a spectrophotometer was used to measure the absorbances of the solution. There was also a recovery portion to check the functionality of the enzyme after being tested under varying temperatures. We had discovered that there were increases in the rate activity of reaction of peroxidase around 4°C and 32°C and that the enzyme had ceased in activity once it reached 60°C. This indicated that the rate of reaction

Read More
901 Words | 4 Pages

The enzymeʼs have an active site that allows only certain substances to bind, they do this by having an enzyme and substrate that fit together perfectly. If the enzyme shape is changed then the binding

Read More
224 Words | 1 Pages

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).

Read More
899 Words | 4 Pages

H20 + 2 O2 This experiment will use 1% catalase solution and 3% hydrogen peroxide solution, both diluted into water so the reaction slows down. Temperature will be controlled in this experiment to change the reaction speed of the enzyme and the substrate, this is what the experiment is looking at. The effect of the temperature will be determined by how much gas is released in two minutes, which will change the pressure inside the test tube and will be measured by a gas

Read More
1167 Words | 5 Pages

5 water bath were set up each to10 °C. (5 were used do the experiment faster) 5 cm3 of starch solution were added into the 5 test tubes that were labeled test tubes. Then 5 cm3 of amylase enzyme was added into the other 5 test tubes that were labeled. Put one of the starch solution test tube (preferably the one labeled 1) and one of the test tube containing amylase into the water bath (10 °C).

Read More
1046 Words | 5 Pages

They can only quicken reactions that will eventually occur, but this enables the cell to have a productive metabolism, routing chemicals through metabolic pathways. Enzymes are very specific for the reactions they catalyze; they make sure the chemical processes go in the cell at any given time. Peroxidase was the enzyme being testing in this experiment. A peroxidase is an enzyme that acts as catalysts, which occurs in biological systems. Peroxidase is found in plants, which they play a role in helping to minimize damage caused by stress factors or insect pests.

Read More
1434 Words | 6 Pages

Enzymes are globular proteins folded into a complex 3-dimensional shape that contain a special surface region called the active site where specific substrate can bind structurally and chemically. They act as catalysts, meaning that they are substances which lower the activation energy required for a chemical reaction to occur and therefore increases the rate of the reaction. Activation Energy is the minimum energy barrier needed to be overcome before a reaction can occur by providing an alternative reaction pathway.

Read More

More about Peroxidase Lab Report

Open Document