Texture of acid milk gels: formation of disulfide cross-links during acidification

Abstract

Denaturation of whey proteins during pasteurization of milk results in the formation of whey protein aggregates and whey protein-coated casein micelles. After cooling a substantial number of thiol groups remains exposed. Formation of larger disulfide-linked protein structures during acidification at ambient temperature was demonstrated by analytical methods. The time-dependent formation of these structures attributed significantly to the mechanical properties of acid milk gels, resulting in gels with an increased storage modulus and hardness. Addition of the thiol-blocking agent N-ethylmaleimide prevented the formation of disulfide-linked structures. The mechanical properties are shown to be the result of the contribution of denatured whey proteins to the protein network as such and the additional formation of disulfide bonds. Surprisingly, these sulfhydryl group-disulfide bond interchange reactions take place at ambient temperature and under acidic conditions. Therefore, the disulfide cross-linking is highly relevant for textural properties of acid-milk products, like yoghurt.