Journal of Food Science · 1997 · 34 citations · 11 references
AgricultureBiochemistryFood ScienceMeat ScienceProtein BiochemistryThermal AnalysisFood GelsMeat QualityProtein AnalysisProteins In FoodsCarrageenanDenaturationMeat Protein DenaturationMeat ProteinsMyofibrillar Protein DenaturationMyofibrillar ProteinsSarcoplasmic ProteinsThermal Stability
ABSTRACT Meat myofibrillar protein (MP) gels and ground pork were used as model systems for studying thermal transition temperatures. Addition of up 2% of κ, ι, or λ 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 (59.4°C), sarcoplasmic proteins (67.8°C), and actin (82.4°C). 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.
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Carrageenan Effects on Salt‐Soluble Meat Proteins in Model Systems
Zoraida DeFreitas, Joseph G. Sebranek, D. G. OLSON et al. · Journal of Food Science · 1997 · 101 citations