Antioxidative ability of chicken myofibrillar protein developed by glycosylation and changes in the solubility and thermal stability

Abstract

Myofibrillar protein prepared from chicken breast muscle was incubated with several concentrations of glucose or maltose for 6h at 60 °C and 35% relative humidity in order to obtain glycosylated chicken protein. When the ratio of the weights of the myofibrillar protein and glucose or maltose had respectively reached 1:6 or 1:3-5, the solubility of each type of glycosylated chicken protein in a 0.1M NaCl solution was exceeded by about 60%, although the myofibrillar protein was insoluble in a low ionic strength solution. Moreover, when the myofibril and maltose reaction (myofibril:maltose = 1:4) was extended to 36 h, the glycosylated protein did not undergo denaturation when held at 50 °C for 2h, while it also exhibited an antioxidative function against superoxide anion radicals.