Protein and water structural changes in fish surimi during gelation as revealed by isotopic H/D exchange and Raman spectroscopy

9 pages, 6 figures.-- Available online Jun 2, 2007.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 H2O 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 D2O, which is consistent with higher water holding capacity in the gel.This work was performed within the Integrated Project SEAFOODplus, partially granted by the European Union under contract No 506359 and the Spanish Ministerio de Educación y Ciencia under project AGL2002-04104-C04-03. The authors (I.S.-G. and A.R.-C.) thank the CSIC for financing I3P grants (European Social Foundation). Our thanks are also due to the electron microscopy service of the Instituto de Ciencias Medioambientales (CSIC).Peer reviewe