Fourier transform infrared (FTIR) spectroscopic study of acid soluble collagen and gelatin from skins and bones of young and adult Nile perch (Lates niloticus)

Abstract Fourier transform infrared (FTIR) spectroscopy was conducted on type A gelatins derived from skins and bones of young and adult Nile perch (Lates niloticus) by a sequential extraction process. Spectra for gelatins were compared to each other and to that of acid soluble collagen from young Nile perch skins, in order to elucidate changes in protein secondary structure during collagen to gelatin transformation. The first gelatin extracts showed diminished amide III bands while the last gelatin extracts showed distinct amide III bands and their amide I bands consisted of a higher percent area of a component around 1690 cm−1. The differences suggested that the collagen to gelatin transition leads to loss of molecular order. The later gelatin extracts exhibited higher molecular order than earlier gelatin extracts, probably because the former contained surviving crosslinks or/and because renaturation of the low molecular weight gelatin fractions (later gelatin extracts) led to formation of more protein–protein linkages.