Abstract
The study was to investigate the role of direct current magnetic field (DC-MF) for water-holding capacity (WHC) of myofibrillar protein gels and to understand potential mechanisms. Samples were subjected to DC-MF with different intensities (3.5, 3.8, 9.5 and 10.4 mT), and DC-MF treatment significantly improved WHC compared with control (46.09%), reaching the maximum value of 50.36% at 3.8 mT. The main reason for the increase in WHC might be that DC-MF modified the protein structure via unfolding, re-crosslinking and aggregation of proteins, which was supported by the increased intensity of tyrosine, aliphatic and tryptophan residues, and reduced reactive sulfhydryl (2.97 to 1.94). And the re-crosslinking between molecules was maintained mainly through hydrophobic interactions and disulfide bonds. Besides, DC-MF treatment helped to generate a relatively loose and uniform microstructure to trap more water as shown by electron microscope image, which was consistent with the highest WHC at 3.8 mT.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
