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 journalArticle

81 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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