| Popis: |
ABSTRACT: Physico-chemical behaviors of natural actomyosin (NAM) from slow-growing Korat chicken (KC) breast and thigh at low (0.2 M) and high (0.6 M) NaCl concentrations were evaluated and compared to those from their corresponding muscles in fast-growing broiler chicken (BC). NAM from KC breast and thigh meat showed higher solubility than their corresponding in BC (p < 0.05). Breast NAM from both chickens showed the highest solubility at 0.4 M NaCl, while thigh NAMs showed the highest solubility at 0.8 M (p < 0.05). SDS-PAGE revealed higher protein extractability for breast NAMs at low ionic strength, regardless of breed and structural protein, particularly troponin, appeared to vary within muscle and breed. NAM from KC showed higher Ca2+–ATPase activity, surface hydrophobicity, but lower total sulfhydryl groups content (p < 0.05). Particle size of NAM solutions varied with ionic strength, in which KC-NAM showed larger size than at lower ionic strength, while BC-NAM appeared to be greater at higher ionic strength. NAM from KC breast showed higher thermal stability as higher initial (T0) and maximum (Tmax) denaturation temperatures of 48.4 and 54.8°C, respectively, recorded by microdifferential scanning calorimetry. The KC-NAM, particularly from breast, exhibited lower turbidity within 40-50°C, while turbidity increased in BC samples at low ionic strength when heated at 60°C. Dynamic rheology revealed different storage modulus (G′) depending on breed, muscle type and ionic strength. Breast BC-NAM formed more elastic gel with higher end point G′ at 80°C (Ge′; p < 0.05). Ionic strength showed reverse effects on different breeds as a stronger Ge′ value achieved in KC- NAM at low ionic strength, while high ionic strength induced stronger gel in BC samples. Aggregation of NAMs began at lower temperatures at higher ionic strength and actin dissociation probably occurred in breast NAM from KC as observed by a drop of G′ at around 70°C. The results of this study revealed differences between NAM of the two breeds, by which higher gel elasticity are expected in KC at lower ionic strength. |
