Effect of fish skin gelatin on gluten proteins during freeze-thaw cycles

Fish skin gelatin (FSG), as a hydrophilic colloid, has the function of protecting the structural characteristics of gluten proteins when added to dough. The effects of varying levels of FSG on the water state, secondary structure, molecular weight and microstructure of gluten proteins before and after three freeze-thaw cycles were investigated using Differential scanning calorimetry, Low-field nuclear magnetic resonance and Fourier transform infrared spectroscopy. The findings indicated that subjecting the gluten to repeated freeze-thaw cycles resulted in disruption of its network structure. Adding FSG promoted cross-linking and aggregation, rebuilding a new gluten network and mitigating freeze-thaw damage. Among these, frozen gluten with 5.0 % FSG addition exhibited the strongest protective effect. Following three freeze-thaw cycles, the freezable water content decreased by 18.4 % and the free sulfhydryl group content by 26.8 % when compared to frozen gluten without FSG. FSG significantly lowered the freezable water content and free sulfhydryl group levels in frozen gluten proteins, leading to reduced exposure of hydrophobic groups, delayed secondary structure transitions, and effective mitigation of structural weakening caused by freeze-thaw cycles. The pores of gluten become shallower and the pore walls become thinner.

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