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bio-113-lab-report-1 - Zach Anderson Edda Cammick Biology...

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Zach Anderson Edda Cammick Biology 113 8 October 2014 Enzyme Functionality Under Different Conditions Such as in the Presence of an Inhibitor, Exposure to Extreme Temperature, and Environments With Varying pH Values Abstract: A series of experiments were conducted to observe how the enzymes amylase and catechol oxidase work. The hypothesis that catechol oxidase would catalyze the reaction between catechol and a potato slice was supported. It could be observed because this reaction caused the potato slice to turn a darker shade. It was also observed that since catechol oxidase needs copper as a cofactor, the use of an inhibitor that binds to copper would cause the enzyme to be unable to function. The enzyme amylase was found to be unable to function if exposed to extreme temperatures and or an acidic or basic pH environment. Introduction: Enzymes are biological catalysts that speed up chemical reactions and are inexhaustible. They can increase the rate at which reactions occur by up to a factor of 10^19. The material that is being acted on by the enzyme is called a substrate. Enzymes work because they can bind to the transition state better
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than the substrate, which lowers the activation energy causing the speed of a reaction to accelerate. The enzyme combines with a substrate at the enzymes active site which creates the enzyme substrate complex. This is where catalysis takes place. When the reaction is complete, the complex dissociates. After the complex dissociates the enzyme is unchanged and as a result can move on to catalyze another reaction. Even though enzymes speed up reactions they do not have the ability to determine the direction of the reaction. Enzyme activity can be affected by many external factors including temperature and pH. For the enzyme amylase, which is involved in the breakdown of starch into glucose and is found in the mouths of humans and a few other mammals, the temperature cannot be too hot or too cold or else it will become denatured and cannot function. The same is true of pH. Amylase cannot function if exposed to a pH that is too acidic or basic. The enzyme catechol oxidase in the presence of oxygen catalyzes the removal of electrons and hydrogens from catechol causing it to be converted to benzoquinone, which polymerizes to form catechol melanin. This melanin causes the darkening of fruits and vegetables therefore when catechol oxidase comes into contact with a fruit or vegetable it turns a darker color. To become active catechol oxidase requires copper as a cofactor. This means that it can be turned ineffective if exposed to an inhibitor. The inhibitor phenylthiourea (PTU) commonly combines with copper. If this occurs the enzyme catechol oxidase is rendered useless.
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Hypothesis: For the following the first sentence is the experimental hypothesis and the second is the null.
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