Biochemistry
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I'm doing an investigation into hydrolysis using urease on CO(NH2)2 + H2O —> CO2 + 2NH3. I was wondering what the best way of doing this was - is a titration is needed as I'm trying to find out how the concentration affects the rate of reaction?
Jenkin writes:
I am assuming you are using the enzyme urease to catalyse the hydrolysis. You might consult Google if you want to find a titration method.
A simpler method which might be useful is to measure 5 cm3 of a urea solution of known concentration (perhaps 0.25M) and add to it about 5 drops of full-range universal indicator. Now add drops of about 0.01M hydrochloric acid until the indicator just turns red.
Do exactly the same with 5cm3 of a solution or suspension of urease.
Now mix the two solutions and start a clock, recording the time when the indicator has turned to a colour corresponding to pH 9 (the ammonia produced will make the solution alkaline).
Repeat the experiment using other starting concentrations of urea. Be patient and be prepared to repeat experiments as the activity of enzyme samples is likely to vary. Whenever possible, compare results obtained using the same enzyme solution on the same day.
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updated: 11 November 2007
