Abstract
Thermal properties and aggregation of natural actomyosin (NAM) extracted from fresh and 9 days ice-stored goatfish were comparatively studied. Myosin of fresh goatfish had the higher thermal stability than that of ice-stored counterpart as indicated by the higher maximum transition temperature ( T max). Additionally, the thermal inactivation rate constant ( K D ) of Ca 2+-ATPase in NAM from fresh goatfish was lower than that of ice-stored counterpart when incubated at the temperature range of 20–40 °C, indicating the lower thermal stability of the latter NAM. NAM from fresh goatfish exhibited the higher turbidity, surface hydrophobicity and disulfide bond formation than did NAM of iced-stored sample when heated at temperature from 35 to 75 °C, suggesting the higher extent of aggregation of the former. However, goatfish NAM showed the lower extent of heat-induced aggregation than did bigeye snapper NAM. As visualized by transmission electron microscopy, network strands of aggregates from bigeye snapper NAM were finer and more uniform than those from goatfish. NAM from goatfish stored in ice showed the lower extent of heat-induced aggregation than did NAM from fresh counterpart. Therefore, heat-induced aggregation of goatfish muscle proteins was governed by freshness.
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