Bio Lab Report - Vu Smiley Vu 003846975 BIO 1510-022 TA...

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Smiley Vu 003846975 BIO 1510-022 TA: Minghui Zeng 18 March 2007 LABORATORY REPORT – ENZYMES Introduction Chemical reactions such as hydrolysis and dehydration synthesis can be controlled by adjusting the points where catalysis takes place. Catalysts are protein-like, although recent studies have shown that some types of catalysis occur due to ribonucleic acid (RNA) molecules. Catalysts basically control earth’s living organisms. Enzymes are biochemicals that are responsible for carrying out the catalysis that occurs in all organisms. The three-dimensional shape of an enzyme allows it to maintain an association between substrates, molecules that will undergo a certain reaction, for a temporary amount of time. If the reaction has large amounts of activation energies, the reaction is very slow. Enzymes, however, are capable of lowering activation energies, thus increasing the reaction rate. In this chemical reaction, the enzymes remain unaltered physically, and therefore, only a small amount of enzyme is required. Enzymes can be reused over and over again. Reaction rates can also be increased by physically, instead of chemically. Increasing the temperature causes molecules to move faster and have a bigger chance for molecular collisions. The reaction rate depends on the concentrations of the substrate and enzyme. Physical and chemical disturbances, that change the enzyme’s three-dimensional shape, ultimately determine if the enzyme is able to catalyze a reaction. Increases in temperature cause the reaction rate to also increase, because increases in heat temperature cause random molecular movement. But if the temperature reaches higher than the optimum, the reaction rate will be slow and therefore, the enzyme denatures. Also, the pH levels of vinegar (pH 3) or pepsin (pH 2) are very extreme and are higher than the optimum pH (6 to 8), and in turn, also denature the enzyme. The substrate amount also can alter the reaction rate: more substrate equals faster reaction rate. But this is true only up to a certain point. Once all the substrate molecules are coupled up with the enzyme molecules, the reaction rate cannot increase any more because it is already at its maximum. And the leftover, uncoupled substrate molecules do not cause the reaction rate to increase. If a graph was drawn of this situation, you would see a point on the graph where the line levels off to look like a plateau, where the enzymes are saturated. The enzyme activity will be examined by using live yeast cells. Living yeast cells are the provider of sucrase, an enzyme that breaks disaccharide sucrose down to a molecule of glucose and fructose. Since sucrose is too large of a molecule to enter into most cells, the yeast will produce sucrase, which hydrolyzes sucrose into smaller monosaccharides that are then able to enter the cell. 1
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This note was uploaded on 04/17/2008 for the course BIO 1510 taught by Professor Rodriguez during the Fall '08 term at Wayne State University.

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Bio Lab Report - Vu Smiley Vu 003846975 BIO 1510-022 TA...

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