ANTIGENIC BEER MACROMOLECULES AN EXPERIMENTAL SURVEY OF PURIFICATION METHODS

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Abstract
The macromolecules of an antigen-rich beer fraction X were characterized by column chromatography. Elution profiles of protein, carbohydrate and immunochemically distinct antigens were recorded after separation on gels of Sephacryl, Sephadex, Sepharose, DEAE-Sephadex, SP-Sephadex, Bio-gel HT hydroxylapatite, Con A-Sepharose, and two types of antibody-Sepharose. The elution patterns demonstrate that beer antigens, originating from barley or yeast macromolecules, can be separated from carbohydrates, from ‘proteose-like’ material and from each other in a few preparative chromatographic steps. Affinity chromatography on a column of immobilized antibodies towards fraction X indicated that the antigenic material constitutes about 25% of the fraction. More than 20% of the protein in fraction X seems to originate from a distinct barley protein Z.