That tends to cover a wide range of polarities. For what it's worth, I purified cyclic peptides from a fungal fermentation using methanol by adsorbing from the broth onto XAD-16, methanol elution, followed by adsorption onto alumina, which was washed with methanol. As they were cyclic, they were fairly neutral in polarity because the amine end was bonded to the carboxylate end.
If you are talking proteins (large molecules), you may consider asking the protein groups here. I'd consider ion exchange or maybe some sort of size exclusion.
I am looking for bioactives as in i want the antioxidant proteins and other potent ones. I read up a bit .There I found for identification of proteins I have break proteins into peptides by digestion with trypsin then mass spectra but i am interested in quantitative separation. Can you please share me your detail protocol if it can be shared.How did you carry outthat fungal fermentation? Thank you very much for your information@JACK SILVER
@Wangkheirakpam, Based on what I see, I'd try seeing if a small amount elutes from silica (dichloromethane/ methanol) . Don't use silica G for this, but try running to 100% methanol (no basic additives- keep it acidic or neutral. Basic polar solvents dissolve silica), then wash the column with methanol to 50% water. Also consider sephadex LH-20, or reverse phase with CHP-20. I don't know which will work best since we don't know the nature of your proteins yet.