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investigating catalase activity
the activity of catalase
investigating catalase activity
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The Enzyme Catalase Experiment
Aim
A series of experiments involving the enzyme Catalase has been
performed in order to determine some of the enzyme's properties. The
enzyme had its reaction rate found in different conditions. Variation
of enzyme concentration, variation of pH, variation of temperature,
and the effect of different concentrations of inhibitors were all
tested.
Increasing the enzyme concentration increased the reaction rate. An
optimum pH and temperature were found for the enzyme, outside of this
optimum the reaction rate would be lower. As inhibitor concentration
rose, the reaction rate fell.
Introduction
Virtually all of the complex biochemical reactions that take place in
animals, plants, and micro organisms are regulated by enzymes. Most
enzymes are Proteins. Each enzyme is able to catalyse only one type
(or a small number) of chemical reactions. Enzymes may only catalyse
reactions which can happen naturally; the substrates do not require
the enzyme but the reaction is much faster in its presence.
In 1965 a theory was created by biologists describing an 'induced fit'
- where the structure of an enzyme is altered by its substrate, by the
movement of charges and hydrophobic/hydrophilic interactions, so the
substrate fits perfectly on the active site in such a way that its
reaction can be catalysed. Once the reaction has ended, the enzyme
returns to its original shape which uses up the least energy to hold
together. It was the work by chemists on the strong and weak chemical
bonds which allowed for this theory to be created. Catalase was
discovered to produce this induced fit in the presence of Hydrogen
Peroxide.
Catalase promotes the breakdown of Hydrogen Peroxide (H2O2) into
non-harmful products, Water and Oxygen by the equation:
CATALASE
2H2O2 ¯ ¯ ¯ ¯ ¯ ¯ ¯ ¯ ¯ ¯ ¯ ¯ ¯>2H2O + O2
Model of catalase structure
As can be seen in the diagram, the Catalase molecule is a very complex
protein. Its structure is held together by a variety of bonds
In the lab, Inhibiting the Action of Catechol Oxidase we had to investigate what type of enzyme inhibition occurs when an inhibitor is added. Catechol oxidase is an enzyme in plants that creates benzoquinone.Benzoquinone is a substance that is toxic to bacteria. It is brown and is the reason fruit turns brown. Now, there are two types of inhibitors, the competitive inhibitor and non-competitive inhibitor. For an enzyme reaction to occur a substrate has to bind or fit into the active site of the enzyme. In competitive inhibition there is a substrate and an inhibitor present, both compete to bind to the active site. If the competitive inhibitor binds to the active site it stops the reaction. A noncompetitive inhibitor binds to another region
Catecholase is an enzyme formed by catechol and oxygen used to interlock oxygen at relative settings, and it is present in plants and crustaceans (Sanyal et. al, 2014). For example, in most fruits and vegetables, the bruised or exposed area of the pant becomes brown due to the reaction of catechol becoming oxidized and oxygen becoming reduced by gaining hydrogen to form water, which then creates a chain that is is the structural backbone of dark melanoid pigments (Helms et al., 1998). However, not all fruits and plants darken at the same rate. This leads to question the enzymatic strength of catecholase and how nearby surroundings affect its activity. The catecholase enzyme has an optimal temperature of approximately 40°C (Helms et al., 1998). Anything above that level would denature the tertiary or primary structure of the protein and cause it to be inoperable. At low temperatures, enzymes have a slower catalyzing rate. Enzymes also function under optimal pH level or else they will also denature, so an average quantity of ions, not too high or low, present within a solution could determine the efficiency of an enzyme (Helms et al., 1998). Also, if more enzymes were added to the concentration, the solution would have a more active sites available for substrates and allow the reaction rate to increase if excess substrate is present (Helms et al., 1998). However, if more
An enzyme is often known as biological catalysts. It acts a substance which speeds up the rate of a chemical reaction but remains unchanged through the process. It works by lowering the activation energy (the amount of energy required to initiate a chemical change) required for a reaction. Enzymes are proteins that are vital to the body because they act as effective catalysts and play an important role within body cells. Enzymes are proteins that are folded into a complex three-dimensional shape that contains an active site where the specific substrate binds structurally and chemically. There are four main protein structures: primary, secondary, tertiary, and quaternary. A primary structure consists of a linear strand of amino acids in a polypeptide chain. They are bonded to one another through covalent peptide bonds. Secondary structures are in coils and folds due to the hydrogen bonds present between hydrogen and oxygen atoms near the peptide bonds. Tertiary structures take a three-dimensional form due to the interaction between amino acids functional groups and disulfide bonds. ...
The first step to the unknown is selecting an actual organism. The best way to select a culture is based on a high-quality distribution. Equally important, shaking up the broth tube facilitates in the distribution. Upon selection, a gram check for purity is performed. Step by step instructions for this procedure can be found in Benson’s, Microbiological Applications p. 99. Furthermore, an aseptic technique must be performed for this test and the entire tests following the unknown. The purpose of this test is to differentiate between gram positive and gram-negative bacteria. The key indicator of gram-positive bacteria is a purple stain and a pink stain for gram-negative bacteria. A slide is viewed with a microscope under oil immersion. Equally
The Effect of Temperature on the Activity of the Enzyme Catalase Introduction: The catalase is added to hydrogen peroxide (H²0²), a vigorous reaction occurs and oxygen gas is evolved. This experiment investigates the effect of temperature on the rate at which the enzyme works by measuring the amount of oxygen evolved over a period of time. The experiment was carried out varying the temperature and recording the results. It was then repeated but we removed the catalase (potato) and added Lead Nitrate in its place, we again tested this experiment at two different temperatures and recorded the results. Once all the experiments were calculated, comparisons against two other groups were recorded.
Investigating the Effect of Substrate Concentration on Catalase Reaction. Planning -Aim : The aim of the experiment is to examine how the concentration of the substrate (Hydrogen Peroxide, H2O2) affects the rate of reaction. the enzyme (catalase).
CaCl2 + H2O + CO2
= 3 ´ E(C-H) + 1 ´ E(C-O) + 1 ´ E(O-H) + 1.5 ´ E(O=O)
from both sides, leaving us with ½ V2 = GH. When the above equation is
Na2S203 (aq) + 2HCl (aq) -> 2NaCl (aq) + H20 (l) + SO2 (g) + S (s)
be yes as I will then be able to use enthalpy change of reaction to
I shall be measuring how much gas is given off. This will be done by measuring the amount of froth on the surface of the liquid. The oxygen released is collected in the form of these bubbles. The equation for the reaction is: (catalase) [IMAGE] H2O2 2H2O + O2 (hydrogen peroxide) (2 part water) (oxygen) I will change the concentration of H2O2 and O2 (making sure the volume stay the same, when one part of a H2O2 particle is taken, an O2 particle is added. Prediction
The Concentration of Hydrogen Peroxide and Speed of The Rate at Which It is Broken Down by Catalase
Electrolysis Investigation Planning In this investigation, I will assess how changing the electric current in the electrolysis of acidified water affects the rate at which hydrogen gas is produced. The solution to be electrolysed is made up using acid and water. It is of little consequence what acid is used however in this case I will use Sulphuric acid (H2SO4). When H2SO4 is put in water it is dissociated and forms ions: H2SO4 → 2H (2+) + SO4 (2-) Ions are also present from the water in the solution: H2O → H (+) + OH (-) During the electrolysis process, the positive hydrogen ions move towards the cathode and the negative hydroxide and sulphate ions move towards the anode.