The effects of -, -, and -carrageenans (CGNs) on the rheological properties, water loss, and ultrastructure of salt-soluble meat protein (SSMP) gels were evaluated. -CGN increased gel strength and water retention of SSMP, suggesting that a molecular interaction may have occurred. However, no indications of specific molecular interactions were observed upon addition of stabilizing/destabilizing reagents. Electron microscopy indicated that improvement of water retention and texture of SSMP/-CGN gels may be due to physical rearrangement of the -CGN and SSMP molecules.

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The effects of κ, ι, or λ carrageenan (CGN), sodium tripolyphosphate (STPP), chloride salts, and meat pH on the freeze/thaw stability of cooked pork sausages were investigated. STPP decreased thaw drip (TD) and increased hardness for all treatments regardless of type of salt or CGN. KCI did not affect the texture of control samples in the presence of STPP, but decreased the functionality of κ‐ and ι‐CGN. Increased meat pH increased the hardness and decreased thaw drip for all CGN treatments, except for λ‐CGN, which remained unchanged. k‐ and ι‐ CGN increased moisture retention of sausages prepared from low‐pH meat.

Meat myofibrillar protein (MP) gels and ground pork were used as model systems for studying thermal transition temperatures. Addition of up to 2% of , , or carrageenan (CGN) to MP caused a very slight change in the thermal denaturation of the meat proteins. Three transition temperatures were found in ground pork samples, which were characteristic of myosin (59.4ЊC), sarcoplasmic proteins (67.8ЊC), and actin (82.4ЊC). Mixtures of high ionic strength had lower thermal transition peaks. CGN did not cause major shifts in transition temperatures, suggesting that molecular interactions between CGN and meat proteins did not occur.