Kriztin27

Hi everyone..how do we make a lipase standard curve of reaction rate vs time? I have 4-nitrophenyl decanoate as my substrate and other buffer and solution such as Tris-HCl, sodium taurocholate and NaCl.

Hi BabcockHall. Thank you for your reply. For the first question, I am actually doing some experiment on lipase using p-nitrophenyl decanoate as substrate. Some studies are using ethanol to stop the enzyme reaction but in the protocol I used, the p-nitrophenyl decanoate is mixed using ethanol first before adding to the assay mixture. I'm curious on how the reaction actually happened. Is it similar with the one using solely p-nitrophenyl decanoate and stopped with ethanol afterwards or differ entirely? For your information, I read the absorbance at 2, 6 and 10 minutes. For the second question, I only want to know whether both of them are similar or different to each other. Thank you.

What happen when p-nitrophenyl caproate mixed with ethanol? Is p-nitrophenyl caproate similar to p-nitrophenyl decanoate?