RP1- Investigstion Into The Effect Of Temperature On The Rate Of Reaction Catalysed By Trypsin Flashcards
What factors influence the rate of reaction of an enzyme-controlled reaction?
Temperature, pH, concentration of the substrate, concentration of the enzyme
These factors can be studied by changing one variable at a time while keeping others constant.
What is the purpose of control samples in the experiment?
To indicate the absence of enzyme activity and to show the colour of a completely hydrolysed sample
One control uses distilled water and the other uses hydrochloric acid.
What is the first step in the method for measuring the effect of temperature on enzyme activity?
Make two control samples
This involves adding milk suspension and either distilled water or hydrochloric acid to flat bottomed tubes.
What is the temperature range used in the experiment to test the enzyme activity?
10°C, 20°C, 30°C, 40°C, 50°C
These temperatures are used to determine the rate of reaction.
How long should the milk samples be equilibrated in the water bath?
5 minutes
This is done before adding trypsin to the samples.
What is the role of trypsin in the experiment?
To hydrolyse the milk samples
Trypsin is added simultaneously to all test tubes after equilibration.
What should be recorded during the experiment?
How long it takes for the milk samples to completely hydrolyse and become colourless
This data is essential for calculating the rate of reaction.
Fill in the blank: The rate of reaction is calculated using the formula: Rate of reaction = _______.
1/mean time
The mean time refers to the average time taken for hydrolysis at each temperature.
Why is it important to keep all other variables constant during the experiment?
To ensure they do not influence the results
This helps in accurately determining the effect of the variable being tested.
Conclusion
- milk contains a protein called casein which, when broken down, causes the milk to turn colourless. Trypsin is a protease enzyme which hydrolyses the casein protein
- as the temperature increases from 10^C, kinetic energy increases so more enzymes substrate complexes form. This means that the rate of reaction increases up to the optimum temperature.
- At temperatures beyond the optimum, bonds in the enzyme structure break which changes the shape of the active site. This means that the substrate and enzyme and no longer complementary.