The role of soluble and insoluble aggregates induced by soy protein isolate (SPI) processing in the gelling properties of myofibrillar protein (MP) was studied. Incorporating soluble SPI aggregate could greatly improve ( P < 0.05) the elastic modulus (G′) and water-holding capacity (WHC) of MP gel, but had no notable effect on MP gel strength. In contrast, incorporating the insoluble SPI aggregate significantly enhanced the G, strength and WHC of MP gel, although the improvement in WHC was smaller than that produced by the soluble aggregate. The results of environmental scanning electron microscopy showed that the soluble SPI aggregate induced a less randomly composite gel structure, which may explain its notable enhancement of WHC. However, the insoluble SPI aggregate appeared to be granules embedded in the continuous MP gel matrix, which may be related to the reinforcement of gel strength. Hence, the results of this study suggest further means of processing commercial SPI for use in meat products.
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