Solid-phase extraction (SPE) procedures for peptide isolation and frac
tionation, based on non-polar and ionic interactions, were evaluated u
sing small synthetic peptides and casein enzymatic hydrolysates. SPE b
ased on hydrophobic phases is a useful, efficient and rapid procedure
for peptide extraction and concentration. It allows a successful pepti
de fractionation using eluents that contain an increasing content of a
cetonitrile in the presence of trifluoroacetic acid. Differences regar
ding selectivity are observed between sorbents. Non-polar interaction
with C-18 sorbents is adequate for the isolation of very polar and hyd
rophobic peptides. CN sorbents are only adequate for very hydrophobic
peptides, PH, CH, C-8 and C-2 sorbents are useful for isolating and fr
actionating hydrophobic and very non-polar peptides, but generally not
for very polar peptides. Ionic solid-phase extraction using Accell Pl
us cartridges of QMA (quaternary methylammonium) and CM (carboxymethyl
) are very useful for the fractionation of peptide mixtures into basic
, acidic and neutral pools of peptides. It can be concluded that SPE u
sing these procedures is a useful tool for the isolation and fractiona
tion of peptides from biological and food samples.