Abstract
The cryoprotective effects of trehalose (w = 0-10%) on washed chicken meat (WCM) were investigated. WCM was produced from broiler, frozen and stored for 360 days on -30 °C. Myofibrillar protein functional stability was monitored by salt extractable protein (SEP) and differential scanning calorimetry (DSC). Salt extractable protein (SEP) showed that the addition of trehalose caused smaller decrease in protein solubility during frozen storage. Peak thermal transition (T p) and denaturation enthalpy (ΔH) of myofibrillar proteins were evaluated. Differential scanning calorimetry (DSC) revealed a shift in peak thermal transition temperature (T p) of myosin and actin to higher temperature as the mass fraction of trehalose increases. The transitions enthalpies of myosin and actin of WCM samples showed higher increase with the increase of mass fraction of trehalose. Since the value of denaturation enthalpy is directly related to amount of native proteins, higher values of ΔH indicates to the higher cryoprotective effects of trehalose.