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

Xiufang Xia, Baohua Kong, Youling Xiong, Yanming Ren

Research output: Contribution to journalArticlepeer-review

162 Scopus citations

Abstract

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 (Tmax) and enthalpy of denaturation (ΔH) (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.

Original languageEnglish
Pages (from-to)481-486
Number of pages6
JournalMeat Science
Volume85
Issue number3
DOIs
StatePublished - Jul 2010

Keywords

  • Freeze-thaw cycles
  • Functional property
  • Microstructure
  • Myofibrillar protein
  • Porcine longissimus muscle

ASJC Scopus subject areas

  • Food Science

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