Abstract
Chicken breasts vacuum-cooked at 75°C were tenderer than those heated at 100°C. There was no significant difference in the amount of hydroxyproline in raw chicken compared with chicken heated at 75°C or 100°C. Scanning electron microscopy (SEM) showed that the degree of shrinkage was similar in the muscle fiber or myofibrils in the samples heated at the two temperatures. No significant difference could be found in the transmission electron microscopic (TEM) observations of myosin aggregation formed by heating at 75°C and 100°C. However, the electrophoresis patterns obtained by using 1-ethyl-3-carbodiimide (EDC) as a zero-length cross-linking reagent indicate that the polymerization of myosin at 100 °C was more advanced than that at 75 °C, suggesting that the aggregates of myosin formed at the higher temperature had a more compact structure. This difference in the state of the myosin molecules may be reflected in the greater shrinkage observed in chicken breast meat heated at 100°C.
