T. Allmere et al., INTERACTIONS IN HEATED SKIM MILK BETWEEN GENETIC-VARIANTS OF BETA-LACTOGLOBULIN AND KAPPA-CASEIN, Journal of agricultural and food chemistry, 46(8), 1998, pp. 3004-3008
Bovine skim milk samples with different phenotypes of kappa-casein (AB
and BB; kappa-cn) and beta-lactoglobulin (AA, AB, and BE; beta-lg) we
re heat-treated at 90 degrees C for different times (1-10 min). The re
sidual native whey proteins in the ultracentrifugal supernatants were
determined by fast performance liquid chromatography using a MonoQ HR5
/5 column at pH 6.2, and the loss of native beta-lg was recorded. The
rate of heat-induced loss of native beta-lg, expressed as the inverted
half-life (1/t(1/2)) of the reaction, was calculated. The reaction di
d not follow true first- or second-order kinetics, varying between the
different genetic combinations. The highest 1/t(1/2) values were foun
d in milk from cows homozygous for kappa-cn B or beta-lg B. The same w
as true after adjustment for differences in casein number. Both the be
ta-lg and kappa-cn genetic variants were found to significantly influe
nce the heat-induced aggregation reaction; with beta-lg having the gre
atest effect. Statistical analysis showed that the two loci for beta-l
g and kappa-cn accounted for more than half of the phenotypic variance
in the experimental groups.