Rheological and Biochemical Characterization of Salmon Myosin as Affected by Constant Heating Rate
Article first published online: 1 MAR 2011
© 2011 Institute of Food Technologists®
Journal of Food Science
Volume 76, Issue 2, pages C343–C349, March 2011
How to Cite
Reed, Z. H. and Park, J. W. (2011), Rheological and Biochemical Characterization of Salmon Myosin as Affected by Constant Heating Rate. Journal of Food Science, 76: C343–C349. doi: 10.1111/j.1750-3841.2010.02024.x
- Issue published online: 1 MAR 2011
- Article first published online: 1 MAR 2011
- MS 20101134 Submitted 10/4/2010, Accepted 11/18/2010.
- dynamic rheology;
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 (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.