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

78 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 1
Externally publishedYes

Fingerprint

Salmon
Myosins
myosin
ionic strength
Osmolar Concentration
Solubility
salmon
solubility
Salts
myofibrillar proteins
hydrophobic bonding
Oncorhynchus tshawytscha
Hydrophobic and Hydrophilic Interactions
salt concentration
salts
Amino Acids
amino acids
Proteins

ASJC Scopus subject areas

  • Food Science

Cite this

Solubility of salmon myosin as affected by conformational changes at various ionic strengths and pH. / Lin, Tein M.; Park, Jae W.

In: Journal of Food Science, Vol. 63, No. 2, 01.03.1998, p. 215-218.

Research output: Contribution to journalArticle

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