Abstract
ABSTRACT Transglutaminase catalyzed crosslinking was initiated in crude actomyosin (refined from surimi processed, mechanically deboned turkey meat – MDTM) at 37°C and 4°C and pH 6.0 and 7.0. Crosslinked reaction products which were analyzed by SDS‐PAGE, indicated a 60% decrease in myosin monomers and a 25% increase in myosin polymers. Polymerization was favored at 37°C. At 37°C, pH did not appear to affect the crosslinking process. However, at 4°C, crosslinking appeared to be enhanced at pH 6.0 over that at pH 7.0. A positive correlation (r = 0.99 and 0.95) was exhibited between the percentage decrease in free amino groups and the decrease in myosin monomer content. Results indicate that guinea pig liver transglutaminase can be utilized to introduce covalent crosslinks in crude actomyosin refined from MDPM.
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