Elucidation of the effect of formaldehyde and lipids on frozen stored cod collagen by FT-Raman spectroscopy and differential scanning calorimetry.
The effect of frozen storage (-10 and -30 degrees 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 degrees C for isolated collagen. Changes in the thermodynamic properties of collagen were observed on frozen storage at -10 degrees C compared with the control at -30 degrees 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 degrees 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 degrees C and -30 degrees C confirmed the alteration of the conformation of collagen not only at -10 degrees C but also in the presence of formaldehyde and fish oil.
Badii
Farah
F
School of Biomedical and Life Sciences, University of Surrey, Guildford, United Kingdom GU2 7XH.
Howell
Nazlin K
NK
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002152:Calorimetry, Differential Scanning; D003094:Collagen / Q000737:chemistry*; D005395:Fish Oils / Q000494:pharmacology*; D005399:Fishes; D005557:Formaldehyde / Q000494:pharmacology*; D005615:Freezing; D012995:Solubility; D013059:Spectrum Analysis, Raman
D000596:Amino Acids; D005395:Fish Oils; D005557:Formaldehyde; D003094:Collagen