E. Molina et al., WESTERN BLOTTING OF NATIVE AND DENATURED BOVINE BETA-LACTOGLOBULIN TODETECT ADDITION OF BOVINE-MILK IN CHEESE, Journal of dairy science, 79(2), 1996, pp. 191-197
Western blotting of bovine beta-LG is a valid method to detect adulter
ation by pasteurized bovine milk, by UHT bovine milk, or by heat-denat
ured bovine whey proteins in cheeses made of milk from other species.
Use of PAGE of whey or isoelectric focusing of beta-LG isolated from t
he casein fraction was followed by immunodetection with anti-bovine be
ta-LG antiserum. The selectivity of the antisera to react with native
and denatured beta-LG was studied. Detection limits of native and dena
tured beta-LG standard solutions were 10 and 50 pg/mu l, respectively.
Immunoblotting of the native-PAGE plates of whey proteins from cheese
allows detection of bovine heat-denatured whey proteins or pasteurize
d bovine milk added to cheese even at <1%. At <1% adulteration by UHT
milk immunoblotting of the isoelectric focusing plates of beta-LG isol
ated from casein micelles is a better detection method. Adulteration w
ith bovine milk or denatured whey proteins in percentages >1% can be d
etected by either Western blotting methods.