Friday, November 1, 2019
Rate of product formation in an enzyme - catalyzed reaction Lab Report
Rate of product formation in an enzyme - catalyzed reaction - Lab Report Example Each and every protein has a specific site or substrate binding and this site remains active at specific pH, temperature and concentration of the substrate. The enzyme active site are specific for the substrates, if some other substrate comes in contact with the enzyme, there will be no ligand ââ¬â receptor complex (Gurung et al., 2013).This is carried out by the ligand ââ¬â receptor complex. The enzyme bound to its substrate, forming enzyme- substrate complex, which became activated. At the end of the reaction, the product is released and the same enzyme is ready to react with other substrate. The enzymes are affected by many external parameters such as pH and Temperature. The alteration of the active site occurs due to the change in pH and temperature. The protein gets denatured and loses its active site. Finally the enzyme activity is lost (Gurung et al., 2013). Catecholase is an enzyme present in plants. Catecholase catalyses oxidation of catechol. Catechol is found behind the skin of many fruits such as apples, potatoes. Catechol molecules on exposure to air, gets oxidized into benzoquinone. Benzoquinone is a brown color substance and changes the solution color to brown. Benzoquinone thus formed inhibits the growth of the micro organisms in the fruits. Catecholase oxidase catalyzes the oxidation of the aromatic group with adjacent phenol groups. This enzyme requires copper ions for the activation. The activity of the enzyme depends on temperature, pH and substrate concentration. The enzyme structure and activity is dependent on the active site and variable groups. The catecholase catalyzed reactions were tested with the given sample. Two test tubes were taken and to each of them 1 ml of potato extract was added. To the test tube named B 2ml of deionized water was added and to the test tube C 1 ml of deionized water was added. To B test
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