Cooked mechanically deboned chicken meat (MDCM), washed with tap water, 0.5% sodium bicarbonate, sodium phosphate buffer (pH 7.2; ionic strength, O.l), or O.lM sodium chloride had increased (PeO.05) gel strength compared to unwashed MDCM. The selected washing solutions affected (PcO.05) lightness (HunterLab L values) of washed meat, and also had a slight (P

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Mechanically deboned chicken meat (MDCM) was subjected to an aqueous washing process with a .5% sodium bicarbonate solution. A screen sieving (.85-mm mesh) separation procedure was incorporated, and two fractions of the washed meat were obtained. One fraction of the washed meat captured by the screen yielded 18.7% of original MDCM on a dry weight basis, and contained 2.8 times more myofibrillar protein and 3.0 times more connective tissue than that of the unwashed MDCM when expressed on a dry weight basis. The fraction of washed meat that passed through the screen sieve device yielded 20.7% of original MDCM on a dry weight basis, and contained 9.2 times more myofibrillar protein than unwashed MDCM. Furthermore, it had 3.0 times less connective tissue than the unwashed MDCM when expressed on a dry weight basis. Thus, the subsequent washed meat fraction would have a composition closely analogous to that of fish surimi. (

Studies were conducted on aqueous washing of mechanically deboned chicken meat (MDCM) with a 0.5% sodium bicarbonate (NaHCO3) solution (alkaline washing, pH 8.4) or a 0.1 M sodium chloride (NaCl) solution (nonalkaline washing, pH 7.0). Decreased enthalpy in myosin transitional temperature was observed in the NaHCO3‐washed meat. Higher expressible water and lower shear values were also observed in heat induced gels from NaHCO3‐washed meat as compared to those from NaCl‐washed samples. Scanning electron microscopy showed more unfolding of myofibrillar proteins of heat induced gels from NaCl washed MDCM as compared to NaHCO3‐washed MDCM. The results suggest that a 0.5% NaHCO3 washing solution provides better heme pigment extraction and results in a whiter meat, but may adversely affect protein functionality.

Ice-slush-chilled versus air-chilled broilers were studied for differences in the heme pigment levels in the gizzard, breast, and thigh muscles. Significant differences (P<05) were observed in pigment levels among the breast, thigh, and gizzard. However, no significant effects on hemoglobin and myoglobin levels were observed between chilling methods. There was a significant difference (P<05) in cytochrome c levels between chilling methods. The observed difference in cytochrome c levels may be a contributing factor in the development of color problems in either fresh or processed poultry meat. Hunterlab L values were significantly (P<.05) negatively correlated (r >-.97) and t^ values were significantly positively correlated (r>.85) with the total heme pigment levels present in the breast muscle. (