Solubility of salmon myosin as affected by conformational changes at various ionic strengths and pH

Tein M. Lin, Jae W. Park

Research output: Contribution to journalArticlepeer-review

89 Citations (Scopus)

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 languageEnglish
Pages (from-to)215-218
Number of pages4
JournalJournal of Food Science
Volume63
Issue number2
Publication statusPublished - 1998 Mar

Keywords

  • Conformation
  • Helix structure
  • Ionic strength
  • Myosin
  • PH
  • Salmon

ASJC Scopus subject areas

  • Food Science

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