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A Step by Step Dilution Where A Solution From A Previous Batchis Diluted by The Same Factor Each Time - E.G. Factor of 10. 10%, 1%, 0.1%..........
A Step by Step Dilution Where A Solution From A Previous Batchis Diluted by The Same Factor Each Time - E.G. Factor of 10. 10%, 1%, 0.1%..........
INDEPEDANT
Temperature,
pH,
Enzyme concentration: Trypsin concentration
Substrate concentration: Milk Concentration
DEPENADANT
Absorbance per second
2). Only the initial rate gets measured because as the reaction progresses, substate concentration
decreases and it is difficult to know the value of the actual substrate concentration whilst the
reaction is. ongoing. And when a decreased substrate concentration is used to calculate the
reaction rate, it won’t be close to the actual rate. So it is inaccurate. This problem gets eliminated
if only the initial concentration is used as the concentration of the reactant is measured and
known before enzymes act on it. That way the reaction rate is accurate.
3.) It is systematic as it is the cuvette that is faulty and damaged. Error is not caused directly by
humans.
ESQ
1).
Take 2cm^3 from a 40 cm^3 of 10% sucrose solution and add it to a second test-tube containing
20 cm^3 of water. Take 20 cm^3 from this solution and add it to a third test-tube containing
20cm^3 of water.
2).
Concentration of trypsin in the soliton is halved with every single consecutive addition.
process is repeated to get a range of concentrations.
3).
Serial dilutions result in more accurate concentrations of the trypsin concentration as it is much
easier method. It also removes the large % error that comes with using very small concentrations of
trypsin to make a soliton, as smaller the substance, greater the % error.
4).
Take 1cm^3 from 1% trypsin solution and add it to 9cm^3 of distilled water. Take 1cm^3 of the
0.1% solution to add it to a test tube containing 9cm^3 of distilled water to make 0.01%
concentration. Repeat the exact same process to make 0.001%.
Log scale