Rheological and biochemical characterization of salmon myosin as affected by constant heating rate

J Food Sci. 2011 Mar;76(2):C343-9. doi: 10.1111/j.1750-3841.2010.02024.x.


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 (S(o)), 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.

MeSH terms

  • Animals
  • Biochemical Phenomena
  • Calorimetry, Differential Scanning
  • Gels / metabolism
  • Hot Temperature*
  • Hydrogen-Ion Concentration
  • Hydrophobic and Hydrophilic Interactions
  • Myosins / chemistry*
  • Myosins / isolation & purification*
  • Protein Denaturation
  • Rheology*
  • Salmon*
  • Seafood


  • Gels
  • Myosins