In this paper, the functional groups in feather keratin obtained by alkaline (NaOH+NaHSO3) and acidic (HCl) hydrolysis, which are considered waste from poultry farms, were determined using infrared spectroscopy analysis. In addition, the Amide I, Amide II, and Amide III regions of chicken feathers were analyzed in depth, and the secondary spatial structure of the protein structure was studied. The presence of the secondary structure of the protein was confirmed by infrared spectra. Spatial conformation graphs were created based on Gaussian deconvolution. According to the results of the study, spectral analysis of feather keratin showed that the main secondary structures of the protein are α-helix and β-sheet. It was also found that β-turn and random coil structures exist, with α helix accounting for a smaller proportion. These results indicated that feather keratin has a partially ordered and partially amorphous structure.
| Mualliflar | D Tursunova, A Maksumova |
|---|---|
| Jurnal | Фармация ва фармакология |
| Nashr sanasi | 2026-07-20 |
| Jild | 2 |
| Son | 16 |
| Betlar | 33-39 |
| DOI | 10.66657/phcc/vol2_iss6-16/art6 |
DOI: 10.66657/phcc/vol2_iss6-16/art6 · Maqolaning asl sahifasi · PDF
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