The measurement of hydrophobic polypeptides in beer using the fluorochrome 1-anilino-8-naphthalenesulfonate

A method has been explored for assessing hydrophobic polypeptides in beer by measuring fluorescence developed upon interaction of the proteins with 1-anilino-8-naphthalenesulfonate. The method was initially applied to three separate purified proteins (bovine serum albumin, cytochrome c and catalase) and different response patterns were observed, suggesting that a simple picture would not be obtained with a complex polypeptide mixture such as beer. Furthermore substantial interference, including a high level of background fluorescence, was caused by beer components, especially in ales. Use of the method, after reducing interference by dilution or dialysis of the beer, does not appear to confer any additional value over the direct measurement of total protein in beer using Coomassie Blue-binding methods.