TY - JOUR
T1 - Concentration-dependent thermal aggregation of muscle salt-soluble protein
AU - Xiong, Youling L.
AU - Blanchard, Suzanne P.
PY - 1992
Y1 - 1992
N2 - 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.
AB - 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.
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M3 - Article
AN - SCOPUS:0141731926
SN - 0023-6438
VL - 25
SP - 544
EP - 547
JO - LWT - Food Science and Technology
JF - LWT - Food Science and Technology
IS - 6
ER -