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

Zachary H. Reed, Jae W. Park

Research output: Contribution to journalArticle

9 Citations (Scopus)

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.

Original languageEnglish
JournalJournal of Food Science
Volume76
Issue number2
DOIs
Publication statusPublished - 2011 Mar 1
Externally publishedYes

Fingerprint

Salmon
Myosins
myosin
Heating
salmon
heat
sulfhydryl groups
disulfide bonds
Differential Scanning Calorimetry
Oncorhynchus tshawytscha
protein aggregates
gelation
hydrophobicity
differential scanning calorimetry
Hydrophobic and Hydrophilic Interactions
Disulfides
purity
turbidity
gel electrophoresis
Electrophoresis

ASJC Scopus subject areas

  • Food Science

Cite this

Rheological and Biochemical Characterization of Salmon Myosin as Affected by Constant Heating Rate. / Reed, Zachary H.; Park, Jae W.

In: Journal of Food Science, Vol. 76, No. 2, 01.03.2011.

Research output: Contribution to journalArticle

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