Yeast Enzyme Lab Report

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Introduction: All organisms depend on the action of enzymes to carry out the reactions of life. According to the text in Campbell Biology, enzymes are biological catalysts. These globular proteins speed the rate at which metabolic processes occur by lowering the activation energy or the energy barrier required to transform reactants to products. Each enzyme is specific, each containing active sites destined for a substrate. Substrates are the reactants or starting materials of chemical reactions. The binding of substrate to active sites orients molecules in a way that promote biological reactions to proceed to form products. The rate of enzyme activity can be impacted by environmental conditions such as material concentration, temperature, and pH. Alterations of these conditions outside normal ranges for an enzyme results in denaturation or shape changes to active sites of enzymes. This results is decreased or cessation of function of the enzyme.(Reece, et al 2014) To investigate this, yeast catalase were incubated at varying temperatures to determine when decreased enzyme activity occurred. Hypothesis included sudden loss of function at temperatures above 45°C.
Methods: Procedures outlined by Dr. John Choinski and Dr. Steven Karafit in Principles of Biology 1: lab notes manual, were followed (Choinski & Karafit, 2016). Temperatures tested included 25, 32, 39, 46 and 53 °C. Each sample was held for 2 minutes at each temperature.
Results: Incubation of yeast catalase provided investigation of enzyme activity. Visual bubbling occurred in each sample with fewer bubbles at 46 and 53° C. A 54% decrease in enzyme activity was seen between control and highest temperature of 53° C. The highest enzyme activity was seen at 32°C, which
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A 54% decrease in activity was recorded between control and highest 53°C temperature tested (mean±SD). Results indicate enzyme disruption occurs between 46-53°C.

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