• Join over 1.2 million students every month
  • Accelerate your learning by 29%
  • Unlimited access from just £6.99 per month

The effect of copper sulphate on the activity of Catalase.

Extracts from this document...


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. 1 Background information Catalase is a globular protein (ENZYME) which catalyses the decomposition of hydrogen peroxide into water (H2O) and oxygen (O2). ...read more.


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. ...read more.


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 1 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 ( 1 ...read more.

The above preview is unformatted text

This student written piece of work is one of many that can be found in our AS and A Level Molecules & Cells section.

Found what you're looking for?

  • Start learning 29% faster today
  • 150,000+ documents available
  • Just £6.99 a month

Not the one? Search for your essay title...
  • Join over 1.2 million students every month
  • Accelerate your learning by 29%
  • Unlimited access from just £6.99 per month

See related essaysSee related essays

Related AS and A Level Molecules & Cells essays

  1. Marked by a teacher

    Investigate the effect of copper sulphate on pepsin activity.

    4 star(s)

    In fact, if the environment surrounding pepsin exceeds pH 6, the pepsin enzyme will be denatured and cannot be used anymore. The optimum temperature for pepsin is that of the human body, around 37 degrees C. it will be fully denatured at a temperature of over 50�C.

  2. Marked by a teacher

    The effect of temperature on catalase activity

    3 star(s)

    In an enzyme catalysed reaction, such as the decomposition of hydrogen peroxide, this increases the rate at which the enzyme and substrate molecules meet and therefore the rate at which the products are formed. As the temperature continues to rise, however, the hydrogen and ionic bonds, which hold the enzyme molecules in shape, are broken.

  1. Effects of Copper Sulphate on the Activity of Catalase

    Catalase contains Fe in its active site. Cu++ may inhibit catalase by displacing the Fe from the enzyme. If the Cu is removed and Fe added back, activity is likely to be restored. This suggests that Cu is a non-competitive inhibitor and it alters the enzyme such that it no longer functions.

  2. An Investigation Into the Effect of Substrate Concentration On the Rate of Enzyme Activity.

    The experiment was also planned thoroughly and some controls were undertaken. The size of the beads and discs was kept the same size and the timing of beads and discs to reach the surface of the hydrogen peroxide was accurate.

  1. The effect of Copper Sulphate concentration on Catalase activity on Hydrogen Peroxide.

    Moreover, the amino acid residues that form the binding site are arranged to interact specifically with the substrate in an attractive manner (electronic complementarity). Molecules that differ in shape or functional group distribution from the substrate cannot productively bind to the enzyme.

  2. Investigate how concentration of the enzyme catalase in celery tissue alters the rate of ...

    Bubbles are also a problem when they are created in the reaction mixture by the addition of a solution from a syringe as the action of squirting from a syringe can create bubbles. Bubbles change the surface area of the reactants (see Variables).

  1. A Level Biology revision notes

    depends on the amino acid sequence o The gene for this sequence is highly polymorphic, having several alleles at each loci o There is great genetic variability between individuals o Thus, antigen is different in other people � injection would cause an immune response o There is only 25% chance

  2. Design an Experiment to Determine the Effects of Copper Sulphate Concentration on the Germination ...

    Gibberellins are plant hormones, which stimulate growth in the embryo of a seed. The embryo releases gibberellic acid and this travels towards its target tissue, the aleurone layer. Here, the gibberellic acid acts as an inducer; it triggers the synthesis and secretion of ? (alpha) and ? (beta) amylase enzymes.

  • Over 160,000 pieces
    of student written work
  • Annotated by
    experienced teachers
  • Ideas and feedback to
    improve your own work