ABSTRACT
Attenuated total reflection Fourier transform infrared spectroscopy (FTIR) has been used to study cross-linking in hard gelatin capsules induced by exposure to formaldehyde, acetaldehyde, and propionaldehyde. These aldehydes are known to cause cross-linking between the amino acid chains of gelatin. Using FTIR spectroscopy, it is possible to analyze the cross-linking mechanisms by studying changes in the vibrational bands of the gelatin spectrum. The FTIR spectrum changes over time when the capsules are left in an aldehyde-rich environment. Analysis of the spectra shows that the early observed spectral changes conform to reaction intermediates proposed in previous work based on nuclear magnetic resonance experiments, specifically, the formation of amine methyl alcohol of arginine and lysine residues. Further spectral changes appear to be mostly from unreacted aldehydes absorbed to the gelatin, although a minor shift of the amide II peak is attributed to cross-link formation.
