An Investigation of the Effect of Catechol Oxidase

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Abstract This experiment tested the effect of enzyme concentration on reaction rate. It is evident that variables that change around an enzyme will change the enzymes ability to function at its optimal level. Changing enzyme concentration will either increase the reaction or rate or decrease it. This depends on how much substrate there is available. If there is more enzyme then substrate then when the substrate is finished the enzyme has nothing to catalyze and so the reaction rate slows down. In this experiment catechol oxidase from potato was used as the enzyme and catechol as the substrate. To find the rate of reaction, the melanoid pigment from solanum tubersome (potato juice) was measured by the intensity of its color. The color was measured using a spectrophotometer at an absorbance of 420 nm. The results showed that as the enzyme had more time to react, the greater the color intensity was and the greater the reaction rate. The highest absorbance read was 0.594 at 8 minutes in test tube 3. The results were consistent in the predictions. Introduction All living cells carry out metabolic activities. These activities provide energy for many other chemical reactions. The rate of these reactions is controlled by enzymes which are tertiary proteins created to catalyze reactions by lowering its activation energy. Every enzyme reaction involves a molecule (substrate) binding to an enzymes active site. This forms the enzyme-substrate complex. Following this, the enzyme substrate complex breaks down producing the enzyme and the products. Each enzyme functions only for a specific substrate. The enzymes shape must be complementary to the shape of the substrate or the reaction will not take place. Since enzymes are perfectly created to perform certain functions. It is important that the catalytic elements in an active site are precisely positioned for their

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