Isolation of beer foam polypeptides by hydrophobic interaction chromatography and their partial characterisation



Beer foam polypeptides have been separated into five groups based on their relative hydrophobicity. Foam stability increases with increasing hydrophobicity of the polypeptide groups. The most hydrophobic polypeptide group contains a large proportion of Coomassie blue-binding polypeptides. Analysis by SDS-PAGE reveals that each polypeptide group is composed of several differently-sized polypeptides. Further purification by anion-exchange chromatography results in five fractions, each of which has a different polypeptide profile on SDS-polyacrylamide gels.