CONDITIONS AND FACTORS THAT AFFECT ENZYME ACTIVITY
INTRODUCTION Catalase is an enzyme found in mammalian tissues and catalyzes the reaction by which hydrogen peroxide (H2O2) is decomposed into oxygen (O2) and water (H2O).(4) Enzyme activity and efficiency is affected by the conditions that the reaction occurs in. Changes in conditions can result in altering of the enzyme’s three dimensional shape and affect the enzyme’s function.(1) The conditions that influence the activity of an enzyme include pH, temperature, substrate concentration(s), ionic strength, and nature of salts present.(2) At a constant set enzyme concentration, the reaction rate increases with increasing substrate concentration until all available enzyme in bound to the substrates, at that point adding more substrate will not further reaction rate.(3)
PURPOSE
The purpose of the experiment conducted was to investigate the effects of various factors and conditions such as pH, temperature, substrate concentration and enzyme concentration on rate of chemical reactions.
HYPOTHESIS
It was hypothesized that the catalase enzyme would decrease in activity after a significant change in temperature, pH, substrate concentration and enzyme concentration from the optimal range of conditions. There are specific conditions in which the enzyme, catalase, will be most effective and have the fastest reaction rate and conditions where the reaction rate will be the slowest. The hypothesis states that the optimal conditions
In this lab or experiment, the aim was to determine the following factors of enzymes: (1) the effects of enzymes concentration the catalytic rate or the rate of the reaction, (2) the effects of pH on a particular enzyme, an enzyme known and referred throughout this experiment as ALP (alkaline phosphate enzyme) and lastly (3) the effects of various temperatures on the reaction or catalytic rate. Throughout the experiment 8 separate cuvettes and tubes are mixed with various solutions (labeled as tables 1,3 & 4 in the apparatus/materials sections of the lab) and tested for the effects of the factors mentioned above (concentration, pH and temperature). The tubes labeled 1-4 are tested for pH with pH paper and by spectrophotometer, cuvettes 1a-4a was tested for concentration and cuvettes labeled 1b-4b was tested for temperature in four different atmospheric conditions (4ºC, 23ºC, 32ºC and 60ºC) to see how the enzyme solution was affected by the various conditions. After carrying out the procedures the results showed that the experiment followed the theory for the most part, which is that all the factors work best at its optimum level. So, the optimum pH that the enzymes reacted at was a pH of 7 (neutral), the optimum temperature that the reactions occurs with the enzymes is a temperature of 4ºC or
This experiment looked at how substrate concentration can affect enzyme activity. In this case the substrate was hydrogen peroxide and the enzyme was catalase. Pieces of meat providing the catalase were added to increasing concentrations of hydrogen peroxide in order to measure the effect of hydrogen peroxide concentrations on the enzyme’s activity. The variable measured was oxygen produced, as water would be too difficult to measure with basic equipment.
peroxide (H2O2). The enzyme breaks H2O2 into water and oxygen. The production of the oxygen
The Effects of Varied Temperatures, pH Values, Enzyme Concentrations, and Substrate Concentrations on the Enzymatic Activity of Catecholase
The goal of this lab was to find the effect of different substrate concentrations of hydrogen peroxide on the rate of catalase enzyme activity. This experiment was specifically meant to find a correlation between an increasing substrate concentration of hydrogen peroxide on the rate of catalase enzyme activity. Four test tubes were used, one filled with 5 milliliters of water and three with 5 milliliters of different concentration of hydrogen peroxide ranging from 0.5%, 1%, and 1.5%. Four drops of yeast solution were dropped into each test tube using a pipette. Then, a lab quest probe was attached to each of the test tubes. The test tubes were tapped twice every second in order to agitate the solution. The rates of the catalase enzyme activities were recorded after 400 seconds of tapping. After the lab, all the materials were cleaned. This experiment was repeated the next day. After both trials were completed, the average from the two trials was taken. Then, the data from the experiment was graphed, with the different substrate concentrations of hydrogen peroxide recorded on the x-axis and the average rates of catalase enzyme activity in kilopascals per second recorded on the y-axis. The experiment results showed that there was a positive correlation
An Investigation on the rate of reaction of the enzyme Catalase on the substrate Hydrogen peroxide.
This experiment was used to determine the effect of varying concentration of hydrogen peroxide on the rate of enzyme activity. This was a decomposition reaction of hydrogen peroxide into water and oxygen gas. The hypothesis of this reaction is that, the rate of reaction will decrease with the decrease of hydrogen peroxide concentration.
The purpose of this experiment was to record catalase enzyme activity with different temperatures and substrate concentrations. It was hypothesized that, until all active sites were bound, as the substrate concentration increased, the reaction rate would increase. The first experiment consisted of five different substrate concentrations, 0.8%, 0.4%, 0.2%, 0.1%, and 0% H2O2. The second experiment was completed using 0.8% substrate concentration and four different temperatures of enzymes ranging from cold to boiled. It was hypothesized that as the temperature increased, the reaction rate would increase. This would occur until the enzyme was denatured. The results from the two experiments show that the more substrate concentration,
The purpose of this investigation is to discover the effect of pH on the activity of catalase, an enzyme which plays the integral role of converting hydrogen peroxide into water and oxygen, and discover which pH level it will work at the most efficient rate (the optimum). The original hypothesis states that that the optimum would be at a pH is 7, due to the liver, where catalase usually resides, being neutral. The experiment consists of introducing the catalase to hydrogen peroxide, after exposure to certain solutions; hydrogen peroxide, water and hydrochloric acids, all containing the adjusted pH, and measuring the height of froth formed, an observable representation of the activity of the enzyme. The final data indicated that
An Enzyme is a protein, which is capable of starting a chemical reaction, which involves the formation or breakage of chemical bonds. A substrate is the surface or material on or from which an organism lives, grows, or obtains its nourishment. In this case it is hydrogen peroxide. This lab report will be explaining the experiment held to understand the effects of the changes in the amount of substrate on the enzyme’s reaction.
Abstract: Enzymes, catalytic proteins that at as catalysis which makes the process of chemical reactions more easily. There are two main factors that actually affects enzymes and their functions which are temperature and pH. Throughout this experiment, the study how pH and peroxidase affects each other and the enzyme was made. The recordings of how the enzymes responded when it was exposed to four different pH levels to come up with an optimum pH which was predicted in the hypothesis and the IRV at the end.
The experiment gave us an insight of how pH affects catalase activity. We hypothesized that the enzyme activity will be quicker near neutral pH levels, than in acidic or basic solutions. The expectation was the optimum rate of enzyme would be at near or at neutral solution, while the rate would be really slow in acidic or basic solutions, such as in solutions of HCl and NaOH. Our experimentation ran into some errors because we used tap water which didn’t have a neutral pH of 7; instead it was 5, which is considered to be acidic. So, our experiment included pH’s of 0, 5, and 13.
Enzymes are high molecular weight molecules and are proteins in nature. Enzymes work as catalysts in biochemical reactions in living organisms. Enzyme Catecholase is found on in plants, animals as well as fungi and is responsible for the darkening of different fruits. In most cases enzymatic activities are influenced by a number of factors, among them is temperature, PH, enzyme concentration as well as substrate concentration (Silverthorn, 2004). In this experiment enzyme catecholase was used to investigate the effects of PH and enzyme concentration on it rate of reaction. A pH buffer was used to control the PH, potato juice was used as the substrate and water was used as a solvent.
In the following experiments we will measure precise amounts of potato extract as well as Phenylthiourea, combined with or without deionized water and in some instances change the temperature and observe and record the reaction. We will also investigate the different levels of prepared pH on varying samples of the potato extract and the Phenylthiourea and record the results. We will answer question such as what is the best temperature for optimum temperature reaction as well as the best pH level for the same reaction.
The purpose of this lab report is to investigate the effect of substrate concentration on enzyme activity as tested with the enzyme catalase and the substrate hydrogen peroxide at several concentrations to produce oxygen. It was assumed that an increase in hydrogen peroxide concentration would decrease the amount of time the paper circle with the enzyme catalase present on it, sowing an increase in enzyme activity. Therefore it can be hypothesised that there would be an effect on catalase activity from the increase in hydrogen peroxide concentration measured in time for the paper circle to ride to the top of the solution.