Protein Oxidation at Different Salt Concentrations Affects the Cross-Linking and Gelation of Pork Myofibrillar Protein Catalyzed by Microbial Transglutaminase

In a fabricated then restructured meat product, protein gelation plays an essential role in producing desirable binding and fat-immobilization properties. In the present study, myofibrillar protein (MFP) suspended in 0.15, 0.45, and 0.6 M NaCl was subjected to hydroxyl radical stress for 2 or 24 h and then treated with microbial transglutaminase (MTGase) in 0.6 M NaCl (E : S = 1 : 20) at 4 and 15 degrees C for 2 h. Protein cross-linking and dynamic rheological tests were performed to assess the efficacy of MTGase for mediating the gelation of oxidized MFP. MTGase treatments affected more remarkable polymerization of myosin in oxidized MFP than in nonoxidized, especially for samples oxidized at 0.6 M NaCl. Notably, the extent of MTGase-induced myosin cross-linking at 15 degrees C in oxidized MFP improved up to 46.8%, compared to 31.6% in nonoxidized MFP. MTGase treatment at 4 degrees C for MFP oxidized in 0.6 M NaCl, but not MFP oxidized in 0.15 M NaCl, produced stronger gels than nonoxidized MFP (P < 0.05). The final (75 degrees C) storage modulus (G') of oxidized MFP gels was significantly greater than that of nonoxidized, although the G' of the transient peak (similar to 44.5 degrees C) showed the opposite trend. Overall, oxidation at high salt concentrations significantly improved MTGase-mediated myosin cross-linking and MFP gelation. This might be because under this condition, MTGase had an increased accessibility to glutamine and lysine residues to effectively initiate protein-protein interactions and gel network formation.