ISOLATION, PURIFICATION, AND ALTERATION OF SOME FUNCTIONAL-GROUPS OF MAJOR MILK-PROTEINS - A REVIEW

This review covers selected methods of isolation and purification of m ainly alpha(s)-casein, beta-casein, kappa-casein, beta-lactoglobulin, and alpha-lactalbumin. Selected methods of alteration of some function al groups of these proteins also were reviewed. Isolation and purifica tion of milk proteins per se are methods of modifying the individual m ilk proteins. Gram quantities of these proteins can now be purified in a relatively short time using ion-exchange resins. Due to the promine nt use of non-food-grade reagents in the procedures for preparation of these milk proteins, individual proteins are not maximally utilized f or the manufacture of food/feed and pharmaceutical products. Therefore , intensive research efforts are needed to obviate the problems associ ated with underutilization of milk proteins.