Determining Optimum Temperature and Ph for Enzymatic Reactions of Alpha Amylase
Enzymes lower the activation energy of chemical reactions but they themselves are not consumed or altered when doing so. These catalysts work best at optimum temperatures and pH's. The temperature and pH at which the reaction occurs the quickest is the ideal condition for the enzymatic reaction.
Alpha amylase converts starch into glucose and when starch is combined with I2KI indicator a dark purple solution forms. As the enzyme breaks down the starch the absorbency will decrease. The absorbency is measured through the spectrophotometer which reads the transmittance of the wavelengths that pass through the solution. In order to determine the optimum temperature for the enzymatic reaction water bath of varying temperatures were made. To determine the ideal pH various buffers were added to the solutions in order to adjust the pH.
At scheduled intervals the reacting solution was added to a cuvette containing I2KI indicator in order to stop the reaction, allowing for accurate readings of absorbency. Once completed graphs which compared absorbency to temperature and pH were created allowing for a visual reference of the results. Optimum temperature and pH were shown determined by noting where absorbency was the lowest because this is where the enzyme catalyzed the most amount of starch. The results showed that alpha amylase most efficiently converts starch into glucose at a temperature of 65C and pH of 5. Therefore, alpha amylase works best in mildly acidic conditions that have a high temperature.
Introduction This experiment tested the cause and effect of environmental factors on enzymes reaction rate. The two environmental factors studied where temperature and pH. Enzymes are catalysts that lower the activation energy of specific reactions without themselves being consumed are altered in any way. When the activation energy is lowered it enables the reaction to be accelerated with less energy expenditure (Campbell, 2002). The rate is determined by speed at
Alpha amylase converts starch into glucose and when starch is combined with I2KI indicator a dark purple solution forms. As the enzyme breaks down the starch the absorbency will decrease. The absorbency is measured through the spectrophotometer which reads the transmittance of the wavelengths that pass through the solution. In order to determine the optimum temperature for the enzymatic reaction water bath of varying temperatures were made. To determine the ideal pH various buffers were added to the solutions in order to adjust the pH.
At scheduled intervals the reacting solution was added to a cuvette containing I2KI indicator in order to stop the reaction, allowing for accurate readings of absorbency. Once completed graphs which compared absorbency to temperature and pH were created allowing for a visual reference of the results. Optimum temperature and pH were shown determined by noting where absorbency was the lowest because this is where the enzyme catalyzed the most amount of starch. The results showed that alpha amylase most efficiently converts starch into glucose at a temperature of 65C and pH of 5. Therefore, alpha amylase works best in mildly acidic conditions that have a high temperature.
Introduction This experiment tested the cause and effect of environmental factors on enzymes reaction rate. The two environmental factors studied where temperature and pH. Enzymes are catalysts that lower the activation energy of specific reactions without themselves being consumed are altered in any way. When the activation energy is lowered it enables the reaction to be accelerated with less energy expenditure (Campbell, 2002). The rate is determined by speed at
Cited: Campbell, N.A. 2002. Biology, 6th ed. Benjamin Cummings, San Francisco, CA Vliet, K.A. 2007. A Lab Manual for Integrated Principles of Biology: Part One – BSC 2010L, 2/e. Pearson Custom Publishing, United States