Effects of alkali and acid solubilization on gelation of characteristics of rockfish muscle proteins

J. Yongsawatdigul, J. W. Park

Research output: Contribution to journalArticle

126 Citations (Scopus)

Abstract

Solubility of rockfish whole muscle and actomyosin was minimum at pH 5 and gradually increased as the pH was shifted to acidic or alkaline pH. Acidic and alkaline solubilization was followed by isoelectric precipitation induced degradation of myosin heavy chain, resulting in a protein band of about 120 kDa. Both myofibrillar and sarcoplasmic proteins underwent denaturation after acidic and alkaline treatment, exhibiting minimal solubility and absence of endothermic peaks. Acid- and alkali-treated muscle proteins readily aggregated upon heating, showing different dynamic rheological patterns compared with whole muscle and washed mince. Disulfide linkages occurred at a greater extent in gel prepared by alkaline solubilization, resulting in higher breaking force and deformation.

Original languageEnglish
Pages (from-to)499-505
Number of pages7
JournalJournal of Food Science
Volume69
Issue number7
DOIs
Publication statusPublished - 2004 Sep

Keywords

  • Actomyosin
  • Alkali/acid solubilization
  • Fish proteins
  • Solubility

ASJC Scopus subject areas

  • Food Science

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