Protein oxidation, a phenomenon that was not well recognized previously but now better understood, is a complex chemical process occurring ubiquitously in food systems and can be induced by processing treatments as well. While early research concentrated on muscle protein oxidation, later investigations included plant, milk, and egg proteins. The process of protein oxidation involves both radicals and nonradicals, and amino acid side chain groups are usually the site of initial oxidant attack which generates protein carbonyls, disulfide, dityrosine, and protein radicals. The ensuing alteration of protein conformational structures and formation of protein polymers and aggregates can result in significant changes in solubility and functionality, such as gelation, emulsification, foaming, and water-holding. Oxidant dose-dependent effects have been widely reported, i.e., mild-to-moderate oxidation may enhance the functionality while strong oxidation leads to insolubilization and functionality losses. Therefore, controlling the extent of protein oxidation in both animal and plant protein foods through oxidative and antioxidative strategies has been of wide interest in model system as well in in situ studies. This review presents a historical perspective of food protein oxidation research and provides an inclusive discussion of the impact of chemical and enzymatic oxidation on functional properties of meat, legume, cereal, dairy, and egg proteins based on the literature reports published in recent decades.
Enzymatic oxidation of acetyltryptophanamide- and tryptophan-containing peptides. Formation of dehydrotryptophan.
