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The reactions were then introduced to I2-KI, which stopped the reactions, at two minute intervals. Each of these trials was repeated three times to ensure proper accuracy.
After concluding the reactions they were placed into a spectrophotometer (A580) for analysis. Graphing the values of the absorbance to time for each pH it was found that the rate of reactions in the neutral pH solutions were much higher than that of the acidic solution. We concluded that this was because of the possibility of an enzyme to become denatured in acidic solution.
Introduction
The study of enzymes is crucial to understanding what drives the forces that create and maintain everything that we consider living...
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Common topics in this essay:
- Monitoring how pH Affects the Rate of Reactions of Barley Amylase
- Reaction Rates of Barley Alpha-Amylase Enzyme with Substrate Starch at Different pH’s and Temperatures
- Determining The Optimal Temperature And Ph Of Barley Amylase
- Reaction Rates of Barley Alpha Amylase with Starch at Specific pH's
- To try to see if the temperature affects the rate in which Amylase breaks down starch into maltose.
- Determining Optimum Temperature and pH for Enzymatic Reactions of Alpha Amylase
- The Wind That Shakes The Barley
- salivary amylase
- planning coursework-starch and amylase
- Investigating The Effect Of Enzyme Concentration On The Rate Of An Enzyme-Catalysed Reaction.
- Chemical Reactions
- Chemical Reactions
- The Sequence Of Chemical Reactions
- Classes of Chemical Reactions
- Chemical Reactions of Copper compounds
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