- In the enzyme reaction with PFAS, how to stop the reaction after a certain time? (I plan to add 1 mL 0.5% methanolic ammonium hydroxide in 0.5 mL reaction solution, will it work?)
- Then I want to dissociate the enzyme from PFAS, and remove the enzyme because I need to measure the PFAS. How to do that? (I plan to freeze (-20 ℃) the sample overnight and then centrifuge it (at 4 ℃) to get the supernatant, will it work?)
Adam B Shapiro
Water-miscible organic solvent (methanol or acetonitrile) or acidification should denature most enzymes, rendering them inactive and allowing the substrates to dissociate. Centrifugation is useful to remove the denatured enzyme. As long as the PFAS is soluble in the supernatant, the method should work. Try it out with PFAS but no enzyme to check the yield of PFAS.
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Zhao Ailin
Add the organic solvent at a volume ratio of 1:4, this time the enzyme will denature, and then centrifuge at high speed to take the supernatant, this is how the serum sample was treated in metabolomics experiments :-）
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