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Investigation of the breakdown of Hydrogen Peroxide by the Enzyme Catalase.

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Introduction

INVESTIGATION OF THE BREAKDOWN OF HYDROGEN PEROXIDE BY THE ENZYME CATALASE AIM: To investigate the breakdown of hydrogen peroxide by the enzyme catalase. PREDICTION I predict that increasing the temperature will increase the rate of oxygen given off. After the optimum point (peak point) the enzyme's shape becomes altered due to high temperatures. The enzyme is said to be denatured and the rate of oxygen will fall rapidly. Summarising my prediction gives. The temperature is proportional to the rate until it reaches it's optimum point were the rate falls. I also predict that the optimum point of the enzyme will be between 50-60 degrees. If I only increase the temperature of the substrate I predict that even more oxygen would evolve this is because when the substrate is at a high temperature the enzyme would not be hot and so it would not be denatured. The enzyme would react quickly to the substrate until it becomes hot and denatured. This would probably last a few seconds, but it would vary from different temperatures. If I only increase the temperature of the enzyme. I predict that less oxygen would evolve because when the enzyme is hot it becomes denatured unlike the substrate, which can take high temperatures. ...read more.

Middle

2 27.0 57.0 74.0 86.0 97.0 105.0 AVERAGRE 29.0 60.0 76.0 90.0 100.0 107.0 70 degrees 30 60 90 120 150 180 VOL .1 23.0 48.0 60.0 76.0 85.0 96.0 VOL. 2 29.0 54.0 66.0 81.0 93.0 102.0 AVERAGRE 26.0 51.0 63.0 79.0 89.0 99.0 80 degrees 30 60 90 120 150 180 VOL .1 19.0 39.0 50.0 58.0 70.0 79.0 VOL. 2 25.0 43.0 54.0 64.0 76.0 83.0 AVERAGRE 22.0 41.0 52.0 61.0 73.0 81.0 Increasing the temperature of only the substrate. Time/seconds 30 60 90 120 150 180 VOL .1 33.0 82.0 93.0 126.0 118.0 126.0 VOL. 2 41.0 69.0 90.0 103.0 122.0 134.0 AVERAGRE 37.0 67.0 86.0 98.0 119.0 130.0 VOL .1 31.0 37.0 40.0 48.0 52.0 57.0 VOL. 2 25.0 29.0 36.0 40.0 48.0 51.0 AVERAGRE 28.0 33.0 38.0 44.0 50.0 54.0 VOL .1 33.0 42.0 53.0 58.0 63.0 71.0 VOL. 2 41.0 50.0 59.0 63.0 72.0 80.0 AVERAGRE 37.0 46.0 57.0 60.0 69.0 75.0 VOL .1 28.0 43.0 56.0 67.0 78.0 89.0 VOL. 2 36.0 63.0 72.0 80.0 86.0 97.0 AVERAGRE 32.0 58.0 69.0 77.0 82.0 93.0 VOL .1 57.0 86.0 98.0 101.0 105.0 115.0 VOL. 2 50.0 76.0 84.0 93.0 97.0 103.0 AVERAGRE 54.0 80.0 92.0 97.0 103.0 111.0 VOL .1 34.0 43.0 56.0 61.0 69.0 73.0 VOL. ...read more.

Conclusion

Non revisable inhibitors They leave the enzyme permanently damaged and so unable to carry out its catalytic function. The bonds maintain the shape of the enzyme molecule. Once broken the enzyme molecule structure becomes irreversibly altered with the permanent loss of its catalytic properties Another experiment, which I could do, is to measure the volume of the mixture of enzyme and hydrogen peroxide before and after the experiment. This experiment could be done by: * Set up the experiment as shown. * Measuring 2ml of catalase and 20ml of hydrogen peroxide. * Pour them in the conical flask and let them react for three minutes. * Make show that in each experiment that the concentration is the same, the temperature is the same and the time is the same. * After the experiment pour the mixture into a measuring cylinder and record the results and find the difference between the volume before and after the experiment. * Try doing the experiment with different temperatures and seeing what happens to the volume of the mixture after the experiment. * You could also do this experiment by changing the concentration. * But make shore that you change one variable each time. 180 142 147 92 120 112 107 99 81 180 130 54 75 93 111 70 88 96 180 138 137 85 116 118 106 97 80 ?? ?? ?? ?? IBRAHIM ELGAYER ...read more.

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