Fractionation and characterization of soluble proteins from cider

摘要

Soluble protein characterization of cider was carried out by reversed-phase high performance liquid chromatography (RP-HPLC) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). RP-HPLC protein separations by means of their hydrophobicity were performed on a C_(18) (250x4.6 mm i.d., 5 μm, 300 A) column, using a mobile phase of acetonitrile-acid-ified water in gradient mode. The protein identifications were carried out by UV spectra analyses. The SDS-PAGE patterns showed several bands with molecular weights between 20000 and 97000 daltons. Several methodologies were tested to isolate and pre-concentrate the cider proteins prior to their separation and detection. The best results were obtained using dialysis to remove low molecular mass contaminants followed by lyophilization to concentrate the proteins.