Abstract
Structural changes of proteins and water during gelation of fish surimi, have been studied by isotopic H/D exchange of water and Raman spectroscopy assisted by monitoring of rheological characteristics, in order to get insights into the structural and functional properties of surimi gels. The results indicate the following: (i) Protein hydrogen bond rearrangements occur involving mainly α-helix to β-sheet transition, (ii) the relative intensity of the symmetric H 2O stretching band near 3220 cm −1 tends to decrease upon gelation, (iii) H/D exchange reveal a slower deuteration kinetics in the gels as compared to the surimi, (iv) the low temperature scanning electron microscopy shows a smaller pore size of the gel network as compared to the surimi, and suggests that water domains in gel are more inaccessible to D 2O, which is consistent with higher water holding capacity in the gel.
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