Concentration-dependent thermal aggregation of muscle salt-soluble protein

Youling L. Xiong, Suzanne P. Blanchard

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


Heat-induced aggregation of chicken breast salt-soluble protein (SSP) was studied in dilute protein solutions (0.2, 0.5, 1.0, 1.5 and 2.0 g/L) containing 0.6 mol/L NaCl and 50 mmol/L sodium phosphate, pH 6.0. Two distinct transition peaks were observed for SSP in protein-protein interaction. Increasing protein concentration from 0.2 to 2.0 g/L decreased the maximum transition temperature from 47.4 to 44.7°C for peak 1, and from 57.6 to 55.1°C for peak 2. Below 48°C, the protein aggregation rate was the highest in the 0.5 g/L SSP solution; above 55°C, the highest rate was with the 1.0g/L SSP solution. The results indicate that the rates and the patterns of heat-induced SSP aggregation were sensitive to the protein concentration and suggest protein-protein interactions may follow different mechanisms at different concentrations of SSP.

Original languageEnglish
Pages (from-to)544-547
Number of pages4
JournalLWT - Food Science and Technology
Issue number6
StatePublished - 1992

ASJC Scopus subject areas

  • Food Science


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