Thermal denaturation of Aulacomya ater ater (Molina) myofibrillar proteins. A differential scanning calorimetric study

PAREDI, MARIA E.; TOMÁS, M.C; CRUPKIN, M; AÑÓN MC

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

AMER CHEMICAL SOC

Lugar: Washington; Año: 1994 vol. 42 p. 873 - 877

0021-8561

Denaturation of the proteins from the adductor muscle of Aulacomya ater ater (Molina) was studiedwith DSC by monitoring maximum temperatures of transitions and denaturation enthalpies. Wholemuscle free of connective tissue showed two transitions (Tm? 50.5 and 72.5 °C) and AH of 2.5 cal/g.Sarcoplasmic proteins contributed to both denaturation peaks. The DSC thermograms of actomyosinwere similar to those of whole muscle. Two endothermic peaks (36 and 50.5 °C) were observed in DSCthermograms of myosin. Paramyosin contributed to myosin transitions. With increasing pH and ionicstrength, the thermal stability of whole muscle decreased. The total denaturation enthalpy significantlydecreased with an increase of the ionic strength