Abstract
The relationship between solubility and conformational changes of salmon (Oncorhynchus tshawytscha) myofibrillar proteins at various Ionic strengths and pH was investigated using myosin as a model system. Solubility of myosin increased with increased KCl concentration up to 0.5M. Further increasing salt concentration resulted In a gradually reduced solubility. In the absence of salt, myosin was slightly soluble at pH>7 or <4. The increased solubility correlated with the Increased surface hydrophobicity and relative sulfhydryl content as well as the decreased α-helicity. At KCl >1.0M, myosin regained its helix structure with a concomitant loss of solubility due to the dominant hydrophobic interaction among nonpolar amino acid residues.
Original language | English |
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Pages (from-to) | 215-218 |
Number of pages | 4 |
Journal | Journal of Food Science |
Volume | 63 |
Issue number | 2 |
DOIs | |
Publication status | Published - 1998 |
Keywords
- Conformation
- Helix structure
- Ionic strength
- Myosin
- PH
- Salmon
ASJC Scopus subject areas
- Food Science