A. Onishi et Mo. Proudlove, ISOLATION OF BEER FOAM POLYPEPTIDES BY HYDROPHOBIC INTERACTION CHROMATOGRAPHY AND THEIR PARTIAL CHARACTERIZATION, Journal of the Science of Food and Agriculture, 65(2), 1994, pp. 233-240
Beer foam polypeptides have been separated into five groups based on t
heir relative hydrophobicity. Foam stability increases with increasing
hydrophobicity of the polypeptide groups. The most hydrophobic polype
ptide group contains a large proportion of Coomassie blue-binding poly
peptides. Analysis by SDS-PAGE reveals that each polypeptide group is
composed of several differently-sized polypeptides. Further purificati
on by anion-exchange chromatography results in five fractions, each of
which has a different polypeptide profile on SDS-polyacrylamide gels.