Recent advances in phosphorylation of food proteins: A review

Phosphorylation is a useful method for improving the functional properties of food proteins. In this article, various methods of phosphorylation are reviewed. Dry-heating phosphorylation, a method developed recently, is also introduced. Some characteristics of phosphate groups are involved, and the effects of phosphorylation on the structural changes, the functional properties, and the physiological functions in vitro of food proteins, are discussed. The types of phosphate linkages and the phosphopeptides from phosphorylated proteins are identified. The molten (partially unfolded) conformations of food proteins formed by phosphorylation are discussed. The phosphorylation of food proteins improved a number of functional properties, including heat stability, emulsifying properties, foaming properties, gelling properties, water absorption capacity, oil absorption capacity, and calcium phosphate-solubilizing ability. In vitro physiological function studies of protein (α-lactoalbumin) indicated that the digestibility (ovalbumin) was improved and the inflammatory response (α-lactoalbumin) was suppressed by phosphorylation. Experiments with animals are necessary to evaluate the toxicity and physiological functions of phosphorylated proteins.