Chicken myofibril gels were formed at pH 6.0 and ionic strength of 0.6 in the presence of calcium chloride (CaCl2) and magnesium chloride (MgCl2). The extractability of salt‐soluble protein (SSP) and myofibril gel strength of leg muscle were increased (P< 0.05) by CaCl2 and MgCl2 and remained constant at 2.5 to 100 mM CaCl2 and MgCl2. The transition temperatures (Tm's) for protein‐protein interaction of leg muscle SSP were decreased (P< 0.05) by CaCl2 but increased (P< 0.05) by MgCl2. Breast muscle SSP extractability and myofibril gel strength were increased by CaCl2 and MgCl2 at less than 5 mM, but were decreased at greater than 10 mM. Tm's of breast muscle SSP were increased (P< 0.05) by MgCl2 but unchanged (P> 0.05) by CaCl2. Moisture loss of breast and leg myofibril gels was at a minimum at less than 5 mM CaCl2 or MgCl2 but increased at greater concentrations of CaCl2 or MgCl2. The divalent cations affected chicken myofibril gelation by changing the extraction and protein‐protein interaction of SSP.
|Number of pages||16|
|Journal||Journal of Muscle Foods|
|State||Published - Jan 1991|
ASJC Scopus subject areas
- Food Science