The Effects of Temperature, Substrate Concentration, and Ph on Catalase Activity

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The Effects of Temperature, Substrate Concentration, and pH on Catalase Activity by Ashley Webber Enzyme Lab Report Thursday 7:30pm October 25, 2012 Megan Duell 1 Abstract The purpose of this experiment was to document the effects of physical conditions and concentration levels on the activity of catalase when exposed to hydrogen peroxide. Namely, we tested the effects of temperature, substrate concentration, and pH levels. The results for the temperature and pH experiments seem to imply 37.5◦ C and a pH of 13 are ideal. The results for concentration level showed an increase in reaction rate with an increase in concentration. However, the data was generally inconclusive. Introduction Enzymes play a critical role in many biological processes. They speed up reaction times and greatly reduce needed activation energy. Without enzymes, many chemical reactions that are necessary for life would take many years to occur. In some instances chemical reactions are 1012 times faster when aided by an enzyme (Nelson et al., 2008). Additionally, without enzymes the ideal temperatures for many necessary reactions are much higher than those found in biological systems (Lerner et al., 2003). Enzymes are proteins characterized by the ability to bind to a substrate, and then once in this enzyme-substrate complex, to change the substrate into a different form. They are usually highly specific and only able to bind to one substrate (Farzin., 2012) Catalase is an enzyme found in nearly all living organisms. Its purpose is to remove toxic hydrogen peroxide from an organism’s cells. It does this by catalyzing the following reaction: 2H2 O2 → O2 + 2H2 O There are hundreds of different types of catalyses with widely varying physical properties and ideal conditions (Chelikani et al., 2004). Things that can affect the rate at which an enzyme catalyzes a reaction can include

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