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The effect of copper sulphate on the activity of Catalase.

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Introduction

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.

Middle

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.

Conclusion

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.

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