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.
Highlights
Surimi is a refined fish protein product containing concentrated myofibrillar proteins obtained by deboning, mincing and washing process from fish fleshes for removal of sarcoplasmic proteins, bloods, lipids and enzymes prior to dehydration and blending with cryoprotectants[1]
The objective of this work was to investigate the structural changes of proteins during gelation of different grades white croaker surimi through tri-step Fourier transform infrared spectroscopy (FT-infrared spectroscopy (IR)) and peak-fitting methods, as well as the observation of their microstructures and texture properties, in order to obtain integral chemical and visual insights into the surimi gelation process involving protein denaturation and the relationship between surimi grades and their gel quality
As IR spectrum is molecular vibrational spectrum, the frequencies or wavenumbers of bands is closely determined by the types of chemical bonds and their modes of vibration
Summary
Surimi is a refined fish protein product containing concentrated myofibrillar proteins obtained by deboning, mincing and washing process from fish fleshes for removal of sarcoplasmic proteins, bloods, lipids and enzymes prior to dehydration and blending with cryoprotectants[1]. Seafood analogous products can be made using surimi, reproducing attributes of natural equivalents For these attributes, gel-forming ability is a crucial functional property determining the unique quality such as sensory and texture[5]. Vibrational spectroscopy is a suitable and rapid method to study the molecular changes in proteins during surimi gelation without complicated preparation. The objective of this work was to investigate the structural changes of proteins during gelation of different grades white croaker surimi through tri-step FT-IR and peak-fitting methods, as well as the observation of their microstructures and texture properties, in order to obtain integral chemical and visual insights into the surimi gelation process involving protein denaturation and the relationship between surimi grades and their gel quality
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