A study of the physicochemical properties of rabbit glycated myofibrillary protein with high solubility in low ionic...

To analyze the physicochemical properties of rabbit glycated myofibrillary protein (GMP) with different solubility ((15.10 ± 0.76)%, (35.03 ± 1.01)%, (55.06 ± 1.25)%, and (75.07 ± 1.86)%) in low ionic strength medium, the changes in SDS-PAGE, foaming properties, emulsifying properties, gelling properties, rheological properties, and thermal stability under different pH conditions were determined. The results indicated that GMP with (75.07 ± 1.86)% solubility had better foaming and emulsifying properties than GMP with (35.03 ± 1.01)% solubility at pH 6.0 and pH 7.5 did; however, GMP with (75.07 ± 1.86)% solubility had lower gel strength and showed more cracks in gel networks. Furthermore, the storage modulus (G') of GMP increased as the solubility increased within the range of (15.10 ± 0.76)% to (35.03 ± 1.01)%, but decreased after the solubility reached (55.06 ± 1.25)%. Results also suggested that the glycation process can improve the thermal stability of myofibrillary protein; GMP with (75.07 ± 1.86)% solubility had the highest denaturation temperature. In conclusion, the physicochemical properties of rabbit GMP were affected by changes in solubility in low ionic strength medium; rabbit GMP with high solubility was more resistant to pH changes than native myofibrillary protein.