Controlled glycation of milk proteins and peptides: Functional properties

Glycation of milk proteins and peptides can be achieved by Maillard-induced conjugation of reducing carbohydrates with the available amino groups of proteins/peptides during the early stages of the Maillard reaction. This conjugation can be achieved under wet or dry heating conditions, with the choice of heating mode influencing the rate and extent of conjugation, in addition to the functionality of the conjugated protein/peptides. Conjugation has been shown to modify the technological and nutritional properties of a range of milk protein/peptide-based ingredients. This review focuses mainly on modifications to physicochemical properties and technological functionality (i.e., solubility, heat stability, emulsification, foaming and gelation properties) of milk proteins and peptides by conjugation. Particular emphasis is placed on understanding of the relationships between changes in protein/peptide molecular structure/conformation, physicochemical properties and technological functionality, as influenced by glycation.