Physicochemical and structural properties of myofibrillar proteins isolated from pale, soft, exudative (PSE)-like chicken breast meat: Effects of pulsed electric field (PEF)

The present study was performed to clarify the effects of pulsed electric field (PEF) on the physicochemical properties and conformations of myofibrillar proteins (MPs) extracted from pale, soft, exudative (PSE)-like chicken breast meat. Various PEF parameters, including the electric field intensity (0–28 kV/cm) and pulse frequency (0–1000 Hz), were varied. The results showed that as the PEF intensity increased, the solubility, surface hydrophobicity and sulfhydryl group content of the MPs were significantly improved. However, when the intensity exceeded 18 kV/cm, these properties declined, which was possibly due to protein aggregation caused by functional group interactions. Additionally, the PEF treatment altered the rheological properties of PSE-like MPs and induced the formation of low-elasticity MPs. However, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated that the primary structure of the MPs was not altered after the PEF treatment. According to the circular dichroism (CD) spectroscopy results, the α-helix contents of the PEF-treated samples were increased but the β-turn and random coil contents were reduced.