ABSTRACTGelation properties were evaluated on high ionic strength soluble (HIS) proteins alone and in combination with low ionic strength soluble (LIS) or insoluble (IN) proteins from beef skeletal, heart, lung and spleen tissues. Apparent stress and strain at failure were greatest in skeletal HIS 6 (w/w) protein gels, followed by heart, lung and spleen. Expressible moisture was greatest in lung HIS protein gels. Microstructures of 6 (w/w) HIS protein gels from skeletal, cardiac and lung tissues were fibrous, while lung HIS protein gels had a globular matrix. Substitution of LIS or IN proteins into HIS protein gels altered expressible moisture, gel microstructure and apparent stress and strain at failure.
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