ABSTRACTHeat induced denaturation and aggregation of plasma protein solutions were studied by low shear viscometry and turbidity measurements. The microstructure of blood plasma gels was evaluated by scanning electron microscopy (SEM). Relationships between gel structure, texture, and waterbinding properties of blood plasma gels prepared under various conditions such as different heating temperatures, pH and protein and salt concentrations were investigated. Generally, it was found that the degree of elasticity and waterbinding properties decreased with an increasing degree of random aggregation of the protein gel network. The degree of aggregation increased with increasing protein and salt concentration and decreasing pH from 9 to 6. With increasing heating temperature from 77° C to 92° C, a partial disruption of the gel structure due to local aggregation phenomena was demonstrated by SEM micrograph
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