The effect of copper sulphate on the activity of Catalase.
The effect of copper sulphate on the activity of Catalase
Aim
The aim of this investigation is to determine how copper sulphate affects the activity of Catalase through the decomposition of hydrogen peroxide into water and oxygen gas. The activity of Catalase can only be determined by the amount of oxygen produced in the decomposition of hydrogen peroxide. If the amount of oxygen produced in an experiment was very high it means that some factors have been kept constant while others have been changed (i.e. favourable conditions).
Under normal circumstances when copper sulphate is not introduced into the reaction the rate of reaction should increase as more substrate is being added into the reaction because the active site of the enzyme (Catalase) is being filled with more substrate particles (H202), in due course, increasing the number of turnover of the Catalase.
In this experiment which will involve copper sulphate the rate of reaction is expected to drop as the concentration of (cuso4) copper sulphate increased because there is not much isubstrate particles present at the active site of the enzyme, because copper sulphate inhibits the active site of the Catalase.
Background information
Catalase is a globular protein (ENZYME) which catalyses the decomposition of hydrogen peroxide into water (H2O) and oxygen (O2).
Catalase (Enzyme) is globular protein which can be classified as biological catalyst, which speed up or control the rate of a chemical or biological reaction in our body, without altering the substrates nor the products neither does it alter the equilibrium between them without itself undergoing any changes.
An enzyme doesn't change during a reaction, what it does is to lower the activation energy of the reaction thereby creating a new route for the reaction to take. This means that the time taken for the reaction normally would have reduced significantly, which by doing these increases the rate of reaction of the experiment (the particles of the substrate and the enzyme collides faster than the usual reaction). The products are formed during the collision. The rate of reaction increases due to some conditions applied which does favour the reaction e.g. temperature, concentration of enzyme & substrate, and inhibitor concentration if applied.
There are a lot of poisonous chemicals formed in the body as by products during metabolic reaction. These chemical wastes could be very harmful to the body tissues and organs of the body, if allowed to accumulate; they cause some very severe damages. In other not to cause this harmful damages there need to be a tool which is going to be able ii2to prevent their accumulation in the body by catalysing their breakdown into less harmful substances, which could be very useful to the body. The tools which perform this function of catalysing these toxic substances are ...
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There are a lot of poisonous chemicals formed in the body as by products during metabolic reaction. These chemical wastes could be very harmful to the body tissues and organs of the body, if allowed to accumulate; they cause some very severe damages. In other not to cause this harmful damages there need to be a tool which is going to be able ii2to prevent their accumulation in the body by catalysing their breakdown into less harmful substances, which could be very useful to the body. The tools which perform this function of catalysing these toxic substances are called enzymes.
Catalase is the enzyme which catalyses the decomposition of hydrogen peroxide (H2O2) into water (H2O) and oxygen (O2). Amongst enzymes, Catalase is got one of the highest turnovers, which is around 5.5 million. Turnover is the number of substrate which an enzyme can bind to, catalyse and form product with, and then releases in seconds.
Each molecule of Catalase has four polypeptide chains, and each is composed of more than 500 amino acids, and within this polypeptide (tetrad) are four porphyrin heme groups like haemoglobin, this provides it with its unique shape, which helps it in the decomposition of H2O2. Hydrogen peroxide is found in the peroxisomse. Hydrogen peroxide is the substrate for Catalase.
Catalase is got one of the highest turnovers and this makes it one of the most widely used enzymes in experiments. A little amount of the enzyme (Catalase) would catalyse a large quantity of substrate within a short period of time.
Reactions (i.e. metabolic activity) would still occur without enzymes, only they would occur too slowly or not at all. All human activity and chemical reactions would take months if not years, while enzymes which are made by all living organisms, makes it a lot faster by decreasing the activation energy/overcoming enthalpy. Since enzymes are globular protein, they have a three dimensional shape which makes it unique and specific to a particular substrate. The polypeptide chains of the Catalase are being held by bonds. These bonds are HYDROGENBOND, IONIC BOND AND DISSULPHIDE BOND 3holding its four polypeptide chains in their four dimensional shape, and this allows it to form receptor sites for its substrate. The shape corresponds with its environment, and it changes with change in temperature, PH.
Enzymes are specific in structure and function because they can only catalyse one particular substance, which fits into their active sites. Active sites are the smallest functional part of an enzyme, which can be called a cleft, contour, or depression, that
Comes in contact, with the substrate. The active site is made up of 3-12 amino acids held together by some bonds of hydrogen and others.
Temperature is one of the factors which affect the quatnary shape of the enzyme. As the temperature of a reaction is increased the rate of collision of the particles of the substrate and the enzyme increases and thus increases the number of product formed per seconds. The temperature of a reaction can be increased by supplying some more energy to the internal energy of the reactants (substances) and through this, the kinetic energy of the particles of each reactant is increased. This increase of particles' kinetic energy increases the rate at which the particles collide because the particles speed as increased, giving rises to more product formation. This energy is given to them by heating or by shaking increasing their kinetic energy.
The increase in the temperature of an enzyme-controlled reaction would bring about an increase in the rate of reaction as stated above up to a certain point or degree. Most enzymes work best at body temperature (37oc-40oc) and any temperature beyond this causes too much vibration and resulting in the denaturisation of the enzyme. At the temperature which enzymes work best is known as OPTIMUM TEMPERATURE. When the temperature for a reaction is too high, the particles of enzyme, vibrate more vigorously, which incorporate the vibration of the enzyme particles holding the bond of the enzyme in place, as enzyme particles vibrate more and more, the force of attraction weakens between the bond and eventually they pull apart. This separation causes a disorganisation in the molecular structure of enzyme, i.e. the distortion of the three dimensional shape. Since the three dimensional shape is distorted, active site is also distorted i.e. disorganised, it is not being held by all it's bond. When substrate molecules come to bind to the active site, there is no binding due to the distortion in shape of the active site, which causes repulsion to the substrate molecule. If there is no enzyme-substrate complex formed, then there is no product formation. And so the particular substrate which is supposed to be catalysed is repelled by the enzyme and there is no more catalysation.
When the temperature of an enzyme is too low, it inactivate, that is it doesn't function any more. It doesn't denaturize all it does is go out of function, but when it is heated again, it start to catalyze substrate again until it reaches its maximum potential.
PH certainly affects the activity of an enzyme, because it affects the precise bonding of the enzyme. Enzymes have an optimum PH, at which they work best.
This optimum PH, came to being because the precise arrangement of the active site of the enzyme is partly fixed by hydrogen bonds between NH2 and COOH group's of the polypeptides which makes up the enzyme.
As concentration of H2O2 increases, the rate of reaction increases because the active site of Catalase is opened to more H2O2 particles. This brings about more collisions and more product formation (more H2O2 with less Catalase).
Inhibition of catalase
FROM BIOLOGY1 BY "MARY JONES" (CHAPTER 7 ENZYMES INHIBITORS AND COURSE OF REACTION) AND ESSENTIAL AS BIOLOGY BY GLENN & SUSAN TOOLE.
2 FROM " ESSENTIAL BIOLOGY" & "ADVANCED BIOLOGY" BY GLENN & SUSAN TOOLE, AND GARETH WILLIAMS
FROM "ESSENTIAL BIOLOGY" & "ADVANCED BIOLOGY" BY GLENN & SUSAN TOOLE AND GARETH WILLIAMS
ii FROM "ADANCEDBIOLOGY" & "ESSENTIAL BIOLOGY" & "BIOLOGY1" GARETH WILLIAMS AND GLENN& SUSAN TOOLE AND Mary Jones chapter 7, effect of concentrations (
