GELATION PROPERTIES OF CHICKEN MYOFIBRILS TREATED WITH CALCIUM AND MAGNESIUM CHLORIDES1

ABSTRACT Chicken myofibril gels were formed at pH 6.0 and ionic strength of 0.6 in the presence of calcium chloride (CaCl 2 ) and magnesium chloride (MgCl 2 ). The extractability of salt‐soluble protein (SSP) and myofibril gel strength of leg muscle were increased ( P < 0.05) by CaCl 2 and MgCl 2 and remained constant at 2.5 to 100 mM CaCl 2 and MgCl 2 . The transition temperatures (Tm's) for protein‐protein interaction of leg muscle SSP were decreased ( P < 0.05) by CaCl 2 but increased ( P < 0.05) by MgCl 2 . Breast muscle SSP extractability and myofibril gel strength were increased by CaCl 2 and MgCl 2 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 MgCl 2 but unchanged ( P > 0.05) by CaCl 2 . Moisture loss of breast and leg myofibril gels was at a minimum at less than 5 mM CaCl 2 or MgCl 2 but increased at greater concentrations of CaCl 2 or MgCl 2 . The divalent cations affected chicken myofibril gelation by changing the extraction and protein‐protein interaction of SSP.