No abstract

Heat-induced gelation, an important functional property of /?-lactoglobulin, was studied by measuring the rheological properties of both the A and B variants of the protein during and after heat treatment within a range of pH, temperature and concentration. Gel electrophoresis was used to determine the extent of denaturation and disulphide bond crosslinking of some samples. Both variants formed gel networks on heating at temperatures > 75 °C, and under most conditions the storage modulus (G') of /Mactoglobulin A gels was higher than the 0' of /?-lactoglobulin B gels, in particular after cooling to 25 °C. A minimum protein concentration of 50 g/1 was required for gel formation at pH 7-0 in 0-1 M-NaCl by both variants at 80 °C. Increasing the protein concentration above 50 g/1 increased G', the extent of increase being much greater for the A variant than the B variant. G' of variant A gels was not much influenced by pH whereas G' of variant B gels decreased slightly from pH 3 to pH 6 and increased between pH 6 and pH 9. When mixtures of the two variants were gelled G' increased at the temperature of heating (80 °C) and after cooling (25 °C) as the relative quantity of variant A was increased. Comparisons of the loss of discrete protein bands from electrophoretic gels (native-PAGE, SDS-PAGE and SDS-PAGE of reduced samples) showed that heating /?-lactoglobulin solutions of 100 g/1 at pH 7 in 0-1 M-NaCl and at 75, 80 and 85 °C caused a faster loss of both native and SDS-soluble /Mactoglobulin A than of /?-lactoglobulin B. It was concluded that the loss of native /Mactoglobulin structure from these solutions during heating was faster than the formation of disulphidelinked aggregates, which was faster than gel formation for both /Mactoglobulin A and /Mactoglobulin B, and that each of these reactions was faster for /Mactoglobulin