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i am planning to hydrolyse glycerol triethanoate and then see how changing the concentration of the enzyme affects the rate of the reaction.
i am using the enzyme lipase.
what would be the best way to do this?
im not sure if i should use the method of saponification because then my catalyst would be NaOH as opposed to lipase.
there is also a titration involved in this which includes making a standard solution, but im not sure what my standard solution should be and why exactly i need to do a titration.
can someone please help me with this? ive somehow got myself REALLY confused!
thank you

2007-10-28 09:37:52 · 1 answers · asked by Anonymous in Science & Mathematics Chemistry

im planning to change the enzyme concentration. i will increase it and decrease it to see if it speeds up the process of hyrolysis or slows it down. the glycerol triethanoate will be the same.
i am also going to use a pH meter as when hyrolysis occurs and the fatty acid is released, the pH increases. from this, you can add an alkali to neutralise the mixture and the rate at which it is added is the rate of hydrolysis.
im just really confused about how i would carry it all out.

2007-10-28 09:38:06 · update #1

1 answers

You need to set up a constant-temperature bath. You should standardize a NaOH solution in the concentration that you will need, against KHP. Your only catalyst is lipase; forget "saponification." You must incubate sealed containers of triacetin and lipase in the constant-temperature bath. Every once-in-awhile, remove ampules from the bath, break them open, and titrate the acid formed. Triacetin + H2O ===> Glycerol + Acetic acid. Acetic acid = H+. Graph [H+] versus time and determine the rate.

2007-10-28 09:52:26 · answer #1 · answered by steve_geo1 7 · 0 0

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