The influence of combined Lysine (Lys) and transglutaminase (TG) on the conformation and gelling properties of oxidatively damaged myofibrillar protein (MP) was investigated. The addition of Lys (5 mM) significantly increased the α-helix content (by 47.8%) and decreased the particle size of oxidatively damaged MP, and improved the cooking yield (by 16.8%) and the breaking strength of MP gels (by 65.5%). The treatment with TG (E:S = 1:500) led to a slightly reduced α-helix content but improved breaking strength (by 41.8%) and cooking loss (by 13.3%) of the gels. Their combination (Lys + TG) showed the greatest and synergistic overall improvement, with the set gel displaying a fine, smooth and compact network structure. Notably, the gelling ability of oxidatively damaged MP upon Lys + TG treatment was significantly stronger than that of non-oxidized MP far exceeding its recovery. Therefore, significantly enhanced gelling properties of oxidatively damaged MP can be attained through the combination Lys and TG.
Keywords: (l)-Lysine (PubChem CID5962); Circular dichroism; Dithiothreitol (Compound CID446094); Linoleic acid (PubChem CID5280450); Microstructure; Particle size; Raman spectra; Rheology.
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