Rheological and Biochemical Characterization of Salmon Myosin as Affected by Constant Heating Rate

Zachary H. Reed, Jae W. Park

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9 Citations (Scopus)


Purified Chinook salmon myosin was studied using sodium dodecylsulfate-polyacryamide gel electrophoresis and densitometric analysis to determine its purity (approximately 94%). Myosin subjected to a constant heating rate began to form aggregates at >24 °C as measured by turbidity at 320 nm. Conformational changes, as measured by surface hydrophobicity (So), began at 18.5 °C and continued to increase up to 75 °C after which it decreased slightly. Total sulfhydryl (TSH) content remained steady from 18.5 to 50 °C after which point the TSH began to drop. Surface reactive sulfhydryl groups gradually increased as the temperature increased from 18.5 to 55 °C and then followed a similar trend as TSH decreased. Presumably disulfide bond started to be formed at around 50 to 55 °C. Differential scanning calorimetry showed 4 peaks, 3 endothermic (27.9, 36.0, 45.5 °C), and 1 exothermic (49.0 °C). Dynamic rheological measurements provided information concerning the gelation point of salmon myosin that was 31.1 °C as samples were heated at a rate of 2 °C/min.

Original languageEnglish
Pages (from-to)C343-C349
JournalJournal of Food Science
Issue number2
Publication statusPublished - 2011 Mar 1



  • Biochemical
  • DSC
  • Dynamic rheology
  • Myosin
  • Salmon

ASJC Scopus subject areas

  • Food Science

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