TitleRheological and biochemical characterization of salmon myosin as affected by constant heating rate.
Publication TypeJournal Article
Year of Publication2011
AuthorsReed, ZH, Park, JW
JournalJ Food Sci
Date Published2011 Mar
KeywordsAnimals, Biochemical Phenomena, Calorimetry, Differential Scanning, Gels, Hot Temperature, Hydrogen-Ion Concentration, Hydrophobic and Hydrophilic Interactions, Myosins, Protein Denaturation, Rheology, Salmon, Seafood

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.

Alternate JournalJ. Food Sci.
PubMed ID21535755