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Effect of ionic strength on the heat-induced soy protein aggregation and the phase separation of soy protein aggregate/dextran mixtures

Li, Xianghong, Cheng, Yunhui, Yi, Cuiping, Hua, Yufei, Yang, Cheng, Cui, Steve
Food hydrocolloids 2009 v.23 no.3 pp. 1015-1023
microstructure, protein aggregates, soy protein, chemical reactions, confocal laser scanning microscopy, turbidity, particle size, rheological properties, sodium chloride, ionic strength, heat treatment, dextran
The effects of ionic strength on heat-induced aggregation of soy protein and phase separation of different soy protein aggregates with dextran were investigated. The increase of ionic strength accelerated protein aggregation as shown by an increase in turbidity, aggregate fraction and particle size of salt-induced aggregates (SA). Adding salt (NaCl) to the aggregates formed at the ionic strength of zero (non-salt aggregates, non-SA), the increase of aggregate size was also found. Zeta potential results evidenced the charge screening effects of NaCl. The results of phase diagrams indicated that the compatibility of mixtures at higher ionic strength was lower than those at lower ionic strength, and SA was more incompatible with dextran than non-SA. The effects of the increase of aggregate size on the phase separation outweighed the ionic strength, which indicated that the depletion interaction also played an important role in the phase separation of soy protein aggregates and dextran. CLSM (Confocal Laser Scanning Microscopy) and rheological observations provided additional information of the microstructures of the mixtures.