Decreased gelling and emulsifying properties of myofibrillar protein from repeatedly frozen-thawed porcine longissimus muscle are due to protein denaturation and susceptibility to aggregation.

The effects of freeze-thaw cycles (FT, 0, 1, 3 and 5 times) on protein functional properties of porcine longissimus muscle were investigated. FT increased gapping between muscle fibres and tore muscle fiber bundles. Myofibrillar protein (MP) isolated from FT muscle showed an increased hydrophobicity (P<0.05), reduced thermal transition temperatures (T(max)) and enthalpy of denaturation (DeltaH) (P<0.05), and enhanced susceptibility to thermal aggregation. These structural changes resulted in major losses in protein functionalities, e.g., 41-43% reductions (P<0.05) in MP emulsifying capacity and emulsion stability after five FT cycles. The ability of MP to form a viscoelastic gel network, as analyzed by small-strain oscillatory rheological testing, also attenuated with FT cycles. The FT process lowered (P<0.05) water-holding capacity (WHC), whiteness, and texture (hardness, springiness, chewiness and cohesiveness) of MP gels. Overall, repeated FT had a detrimental effect on the general functionality of porcine MP, and protein denaturation and aggregation were implicated in the functionality losses. Copyright 2010 Elsevier Ltd. All rights reserved.