Abstract
A developed Fourier transform infrared spectroscopy (FT-IR) was employed to investigate changes of protein conformation, which played significant roles in maintaining stable protein networks of white croaker surimi gel, exploring the relationship between protein conformation and surimi gel networks. Spectra of surimi and gels with different grades (A, AA, FA and SA) were analyzed by tri-step FT-IR method and peak-fitting of deconvolved and baseline corrected amide I bands (1600~1700 cm-1). The result showed that α-helix was the main conformation of surimi proteins. During surimi gelation, α-helix of myosin partially transformed into β-sheet, β-turn and random coil structures. β-sheet and random coil structures were the main protein conformations maintaining the structure of surimi gel, of which β-sheet made the main contribution to gel strength. Scanning electron microscopy (SEM) result revealed that surimi gels had a fibrous and homogeneous network structure. Moreover, ordered interconnections between three-dimensional proteins networks of gels were inclined to emerge in higher grade surimi, in agreement with the gel strength results. It was demonstrated that the tri-step FT-IR spectroscopy combined with peak-fitting could be applicable for exploration of surimi protein conformation changes during gelation to deepen understanding of its effect on gel quality.