Abstract
The effect of frozen storage (−10 and −30 °C), formaldehyde, and fish oil on collagen, isolated from cod muscle, was investigated. Salt- and acid-soluble collagen fractions as well as insoluble collagen indicated changes in solubility on frozen storage. Differential scanning calorimetry (DSC) showed a highly cooperative transition at 28.2 °C for isolated collagen. Changes in the thermodynamic properties of collagen were observed on frozen storage at −10 °C compared with the control at −30 °C because of changes in structure. In the presence of formaldehyde, there were no changes in the DSC collagen transition; however, in the presence of fish oil there was an increase in enthalpy and an extra peak was observed at 44.6 °C, indicating collagen−fish oil interaction. Structural changes resulted in a decrease in the solubility of collagen in salt and acid solution. FT-Raman spectra obtained for collagen at −10 °C and −30 °C confirmed the alteration of the conformation of collagen not only at −10 °C but also in the presence of formaldehyde and fish oil. Keywords: Fish fillets; cod; frozen storage; collagen extractability; amino acids; differential scanning calorimetry; FT-Raman spectroscopy

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