A COMPARISON OF THE RHEOLOGICAL CHARACTERISTICS OF DIFFERENT FRACTIONS OF CHICKEN MYOFIBRILLAR PROTEINS

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Abstract

ABSTRACT Suspensions of myofibrils and salt‐soluble (SSP) or insoluble (SIP) proteins of chicken breast muscle in 0.6 M NaCl at pH 6.0 were heated to induce gels. Dynamic oscillating measurements showed multiple transitions in the shear storage modulus and loss modulus for all three protein fractions in the temperature range of 40–65C. However, changes in these viscoelasticities were most pronounced for SSP and least appreciable for SIP. Gel penetration test also revealed a descending order of SSP < myofibrils < SIP in gel strength. The three fractions of myofibrillar proteins appeared to follow a similar gelation mechanism but vary in the density of the gel networks.

Original languageEnglish
Pages (from-to)217-227
Number of pages11
JournalJournal of Food Biochemistry
Volume16
Issue number4
DOIs
StatePublished - Aug 1992

ASJC Scopus subject areas

  • Food Science
  • Biophysics
  • Pharmacology
  • Cell Biology

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