Contribution of protein conformation and intermolecular bonds to fish and pork gelation properties

Fish and pork paste gels were produced by various heat treatments. Gelation properties were evaluated by textural analysis and measurement of cooking loss. Raman spectroscopy was employed to monitor the structural changes of proteins during gelling, and intermolecular bonding as a function of temperature was measured. Pre-incubation at 40 °C significantly increased the breaking force of the cooked fish sample, but had little effect on the breaking force of the cooked pork sample. In addition, incubating pork paste at 40 °C could decrease the cooking loss of the cooked pork sample. The differences were intimately associated with changes in protein conformation (α-helix and β-sheet) and intermolecular interactions (hydrophobic interaction, disulfide bonding and non-disulfide covalent crosslinking) during gelling.