Abstract
This paper describes an experiment to determine …………….
Introduction
Enzymes are made from proteins. They are biological catalysts that speed up the rate of chemical reaction by lowering the activation energy of the reaction. Enzymes are precise and catalyze only detailed reaction. Specificity is an outcome of active site of enzyme that acts on the substrate. Catecholase, which catalyzes a reaction in which catechol, then catechol becomes the product called benzoquinone, which is a reddish-brown color, which make it easier to determine the quantity that has been formed. (Dickey). Moreover, the enzyme activity is persuaded by ph, plus temperature. Change in ph will have effect on hydrogen bonding that can modify the form of protein. Increase in the temperature will spread the reactions rate; nevertheless, if the temperature is unreasonably high the enzymes will denatures. For this experiment we use spectrophometer that measures the color intensity of the solution for particular wavelength. In addition, finding a specific enzyme called Catecholase, as well as the activity of Catecholase in optimal and denaturing environments.
A detailed enzyme termed Catecholase is dependable for the brown bruising of fruits and vegetables when they are exposed to oxygen. Catecholase does this by catalyzing a reaction among catechol and oxygen, in which catechol is oxidized to benzoquinone and oxygen is reduced to water. Hypothesis: The accumulation of Catecholase (an enzyme) to catechol (substrate) will result in the creation of Benzoquinone.
Materials & Methods Adjusted the spectrophotometer with blank solution, then measured 1ml of Catecholase (potato extract) in the test tube B, using 1 ml graduate pipette and added 5 ml of distilled water. Protected the test tube with Parafilm and mixed the content. On the spectrophotometer, arranged the wavelength to 540 nm, formerly inserted the test tube into sample
References: Works Cited Encyclopedia. Enzymes. 17 April 2012 . Dickey, Jean. Laboratory Investigations For Biology. 2nd ed. San Francisco: Benjamin Cummings, 2003. Print.