National Academy of Agricultural Sciences (NAAS)
 |
PRINT ISSN : 2319-7692 Online ISSN : 2319-7706 Issues : 12 per year Publisher : Excellent Publishers Email : editorijcmas@gmail.com / submit@ijcmas.com Editor-in-chief: Dr.M.Prakash Index Copernicus ICV 2018: 95.39 NAAS RATING 2020: 5.38 |
Studies were undertaken on the feather of broiler chicken of six to eight weeks of age and culled White Leghorn birds above 64 weeks of age, slaughtered at Meat Technology Unit, Mannuthy. The feather samples were collected from a total of 24 birds comprising of six males and females from the broiler and layer groups. In the present study the amino acid composition of both broiler and layer chicken feather keratin consisted of both hydrophilic and hydrophobic amino acids with high serine content (12.40 per cent), followed by glutamine (9.65 per cent), cystine (7.68 per cent), glycine (6.85 per cent), leucine (5.62 per cent), aspartic acid (5.55 per cent), proline (4.52 per cent) and valine (4.21 per cent). It was seen that the feather fibre consisted of more hydrophobic amino acids than hygroscopic in both broiler and layer birds. The FTIR-ATR (Fourier Transform Infrared Spectroscopy- Attenuated Total Reflectance) spectrum of feather of broiler and layer chicken feather showed characteristic bands of proteins, related to the keratinous material. The amide I, II and III band were shown in between the range of 1700 - 1600 cm-1 with a peak at 1631 cm-1; 1600–1500 cm-1 with a peak at 1540 cm-1and 1330–1200 cm-1 with a peak at 1232 cm-1 respectively. In all samples the peak intensity of amide II bands was lesser than the amide I peak. There were no major differences in the chemical structures between broiler and layer samples. The results of the present study confirmed that both broiler and White Leghorn chicken feathers could be beneficiated as a good source of protein.
 |
 |
 |
 |
 |
