Properties of Glycated Chicken Myofibrillar Proteins with Enhanced Antioxidant Abilities

Abstract

Antioxidant properties were observed following glycation of chicken myofibrillar proteins (Mfs) with maltose, via the Maillard reaction. We then improved the conditions of the Maillard reaction, including temperature, relative humidity, reaction time, and the weight ratio of protein-maltose, to obtain glycated chicken Mfs with enhanced antioxidant ability, and found that the incubation conditions of 65℃, 41%, 36 h, and 5, respectively, induced higher antioxidant activity. Under these conditions, the superoxide anion radical-scavenging activity (SOSA), converted on the basis of the SOD IC 50 value (1.5 U/mL), of 541 U/g of protein was similar to that of dried Delaware grape (700 U/g). Interestingly, the SOSA was halved following partial pepsin digestion, although the solubility increased from 31.5 to 58.5%, suggesting that the primary structure or specific peptide sequences, irrespective of the shape of protein, may contribute to the antioxidant ability of glycated chicken Mfs.