title: Rheological and biochemical characterization of salmon myosin as affected by constant heating rate.
abstract: 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.
authors.affiliation: Oregon State Univ, Seafood Research and Education Center, 2001 Marine Drive Rm 253, Astoria, OR 97103, USA.
authors.forename: Zachary H
authors.initials: ZH
authors.lastname: Reed
authors.forename: Jae W
authors.initials: JW
authors.lastname: Park
mesh_terms: D000818:Animals; D001669:Biochemical Phenomena; D002152:Calorimetry, Differential Scanning; D005782:Gels / Q000378:metabolism; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D009218:Myosins / Q000737:chemistry* / Q000302:isolation & purification*; D011489:Protein Denaturation; D012212:Rheology; D012474:Salmon; D017747:Seafood
chemical_list: D005782:Gels; D009218:Myosins