Abstract
Mechanically separated chicken (MSC) was obtained by two different separation methods (MSC1, Beehive separator, 3–5 d-old bones; MSC2, Poss separator, fresh bones) and compared to chicken breast trim (CBT). Rheological attributes of myofibrillar protein solutions during thermal gelation and cooling were evaluated. All sources exhibited gelation with increased temperature (decreased δ). In all three treatments, a peak, decline, and subsequent increase in both the G′ and G″ was observed in the 50–55 °C range, with peak values being higher for CBT than for both MSCs. G′ slopes on both sides of the peak (S2, S3) and following the decline (S4) were significantly different between CBT and both MSCs (P < 0.05) and indicated greater instability of the solid-like structure in the temperature range of 50–55 °C (myosin rod denaturation). Myofibrillar protein profiles confirmed fiber type differences among materials, as well as greater myosin fragmentation or modification in the MSC samples.
Published Version
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