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

@article{Xia2010DecreasedGA,
  title={Decreased gelling and emulsifying properties of myofibrillar protein from repeatedly frozen-thawed porcine longissimus muscle are due to protein denaturation and susceptibility to aggregation.},
  author={Xiufang Xia and B. Kong and Y. Xiong and Yanming Ren},
  journal={Meat science},
  year={2010},
  volume={85 3},
  pages={
          481-6
        }
}
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… Expand
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TLDR
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