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Hair or bristle is one of the key by-products of humane slaughter of pigs. In the present study, Fourier-transform infrared (FTIR) spectroscopy was used for examining protein secondary structure of hair fiber from different breeds of pigs (Ghungroo, Ninag Megha, Hampshire, and Duroc). Prominent amide I (1635–1648 cm −1 ) and amide II (1517–1528 cm  −1 ) bands could be observed in the spectra. Differences in presence/absence of certain FTIR bands between breeds suggests influence of genetic background in the structure of hair fiber. Deconvolution resolved secondary structure of protein in amide I region of spectra into corresponding α-helix (38.0 ± 2.9%), β-sheets (32.2 ± 2.0%), β-turns (19.4 ± 3.1%) and unorganized structural components (10.3 ± 2.5%). Heating of fibers from 80°C to 120°C resulted in changes in amide regions and α-helix to β-sheet ratio of amide I band. Further, correlations were calculated between area under the curve of various FTIR bands and tensile properties of the fiber. Area of FTIR band at 1635 cm  −1  was positively correlated with tenacity, initial modulus, extensibility, and work of rupture (r = 0.30 to 0.39). In nutshell, the study reveals subtle differences in secondary structure of hair with respect to breed or temperature treatment and suggests relation between FTIR spectral characteristics and tensile properties.

Characterization of Secondary Structure of Pig Hair Fiber Using Fourier-transform Infrared Spectroscopy