文摘
Glycation of whey proteins leads to changes of the nutritional and functional properties of the proteins. Lactosylation of ¦Â-lactoglobulin was monitored under conditions varying with respect to temperature, water activity (aw), and pH. The rate of the overall lactosylation and the average lactosylation degree increased with temperature (50-70?¡ãC) and aw of 0.51-0.64, but were only slightly affected by reaction mixture pH (pH?5-7) before drying. The reaction seemed to occur in two phases, the transition between which was related to a lowering of the glass transition temperature of the system. Detailed kinetic analysis of the initial step showed that the pseudo first-order rate constants for formation of mono-lactosylated ¦Â-lactoglobulin in general were higher than the rate constants for formation of di-lactosylated ¦Â-lactoglobulin. However, the temperature dependencies of the two reaction steps were similar, corresponding to an activation energy of about 100?kJ?mol?.