Beer fluorescence and the isolation, characterisation and silica adsorption of haze-active beer proteins

The fluorescence spectra and lifetimes of diluted beer have been explored and found not to report on protein removal either by silica or tannic acid, nor polyphenol uptake by PVPP. Comparing the fluorescence spectra of beer with that of tea and hops, it seems that proteins, complex polyphenols and iso-alpha-acids can contribute to the intrinsic fluorescence of beer, although the contribution from polyphenols must be minimal since treatment with PVPP does not dramatically change the background fluorescence. To eliminate the problem of background fluorescence haze-active protein was isolated. Steady-state and time-resolved fluorescence techniques were used to characterise these and to monitor their uptake by different silica gels as a function of pH. Heat treated large pore volume, small surface area silicas were the more effective adsorbers for the proteins under study, with pH 4 being optimum. Using both intrinsic amino acid fluorescence and the extrinsic fluorophore fluorescamine, the time-resolved fluorescence anisotropy has been measured and the radius of the isolated haze protein found to be similar to 35 Angstrom. Comparisons have been made with proteins of known size and structure such as human and bovine serum albumins (HSA and BSA).