An Experimental Investigation On Enzymes

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Enzymes are catalytic proteins that act to speed up chemical reactions that occur in our bodies and in the bodies of many other organisms by reducing the amount of activation energy required in order for a reaction to occur. Without enzymes, the chemical reactions that take place in all organisms would take place too slowly to keep the organism alive. Since all enzymes are proteins, and protein’s functions are dependent on their structure, enzymes require certain conditions to maintain their perfect structure. The disorder of structure and function of an enzyme is known as denaturation. Certain factors such as temperature, pH, enzyme concentration, and substrate concentration have certain effects on enzyme activity. To investigate the effects of these different conditions, an experimental investigation was set up to test the four different variables and their effect on the enzyme catecholase as it catalyzes catechol, the solute. Results can be seen on Figures A – D.
Figure A shows the data collected when an enzyme’s reaction rate, in other words, absorbance, is measured at varying temperatures. Beginning with an absorbance of 0.549, the enzyme, catecholase, shows an inversely proportional relationship between its absorbance and increasing temperature. Our data shows that as the enzymes are subjected to higher temperatures, the enzymes are rendered inactive and therefore denatured. On the other hand, the enzyme’s optimal potential is shown somewhere between 10˚C and 24˚C.
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