Abstract
Polypeptides from beer and from aqueous extracts of barley have been separated by hydrophobic interaction chromatography. The most stable foams are given by polypeptides of greatest hydrophobic character whereas hydrophilic polypeptides give much less stable foams. This effect is most pronounced in polypeptides of molecular size between 5000 and 30,000 and less so in the case of high molecular weight polypeptides (> 50,000).
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