Influence of genetic variants on surface-active properties of caseins
1997
Gao, H. | Britten, M. | Ng-Kwai-Hang, K.F. (McGill Univ., Ste Anne de Bellevue (Canada). Dept. of Animal Science)
The objectives of this work were to determine whether genetic variants had an influence on the time-dependent changes in surface tension for dilute solutions of alphas1-casein, beta-casein and kappa-casein. Whole caseins were prepared by iso-electric precipitation from the skim milk of cows to provide different phenotypes of the above caseins. Anion exchange chromatography was used to fractionate the individual caseins which were desalted and lyophilized. Approximately 0.005 per cent (w/v) solutions of the proteins were prepared in 0.01 M phosphate buffer. A Wilhelmy surface balance was used to measure surface tension of the dilute protein solutions maintained at 22 more or less 0.1 degree C for 60 min. The surface tension-time curves indicated that both the types of caseins and genetic variants within a specific casein influenced the rate and extent of lowering of surface tension by those proteins. Beta-casein exhibited the largest and most rapid lowering of surface tension than kappa-casein and alphas1-casein. Within the beta-casein, the kinetics of the surface tension decay were in the following descending order according to phenotypes: A1A1 more than A1 A2 more than A2A2 more than BB more than A2B more than A1B. The ranking was AB more than AA more than BB for kappa-casein and CC more than BB more than BC for alphas1-casein.
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