Abstract
Thermal stability of ground chicken meat and myofibrillar proteins mixed with κ-, ι-, and λ-carrageenan (CGN) at different NaCl concentrations was investigated with differential scanning calorimetry. Three transitions, characteristic of myosin head (63.3, 62.2°C), sarcoplasmic proteins/myosin tail (67.7, 68.6°C), and actin (78.3, 81.4°C), were observed for nontreated thigh and breast muscles, respectively. The influence of CGNs on the thermal transitions was dependent on salt concentrations. κ-CGN with 2.5% NaCl decreased (P < 0.05) transition temperature (Tmax) of thigh myosin head and actin, while all three CGNs with or without 2.5% salt decreased (P < 0.05) Tmax for breast actin. Total enthalpy of denaturation decreased slightly in the presence of κ-CGN for thigh muscles only. The gum effects on myofibril isolates were variable and were salt-dependent. The results suggested molecular interactions between the gums and meat proteins, but the response of the specific proteins to gums appeared to be muscle type-dependent.
| Original language | English |
|---|---|
| Pages (from-to) | 247-253 |
| Number of pages | 7 |
| Journal | Food Research International |
| Volume | 34 |
| Issue number | 2-3 |
| DOIs | |
| State | Published - 2001 |
Keywords
- Carrageenan
- Chicken proteins
- Thermal stability
- Thigh and breast muscles
ASJC Scopus subject areas
- Food Science