Scanning Calorimetric Behavior of Tilapia Myosin and Actin due to Processing of Muscle and Protein Purification

ABSTRACT The thermal behavior of tilapia muscle proteins was investigated by differential scanning calorimetry at various stages in the processing of surimi and during purification of myosin and actin. A shift in the thermal transition of actin to lower temperature was observed and the enthalpies of denaturation for both actin and myosin decreased with further processing. Salt addition also induced shifts in denaturation transitions to lower temperatures and decreased enthalpies of denaturation.