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Journal : Communications in Science and Technology

Ionic liquid ultrasound-assisted extraction (IL-UAE) for duck feather keratin and in silico evaluation as a potential procollagen n-endopeptidase inhibitor Sianita, Maria Monica; Kusumawati, Nita; Asri, Mahanani Tri; Dzulkarnain, Shod Abdurrachman; Al Hafidl, Achmad Naufal; Kahfi, Ashabul; Nabila, Mutiara Azfa; Setiawan, Ferdiansyah; Isyrak, Luthfiyah; Rahmawati, Khofifatul
Communications in Science and Technology Vol 10 No 1 (2025)
Publisher : Komunitas Ilmuwan dan Profesional Muslim Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.21924/cst.10.1.2025.1669

Abstract

This research aims to optimize keratin extraction from duck feathers using an eco-friendly ionic liquid-ultrasound-assisted extraction (IL-UAE) method and evaluate its potential applications in tissue engineering. It investigated the effects of deposition pH (1-6), ultrasonication temperature (40-60°C), and time (60-180 min) on extraction yield and physicochemical properties. The results demonstrated the optimal extraction conditions at pH 3, 40°C, and 60 minutes, yielding 82% keratin with a 0.50 mg/mL concentration, while the lowest yield production was found at pH 6 (33%, 0.20 mg/mL). Meanwhile, characterization via FTIR confirmed predominant ?-sheet structures with characteristic peaks at 3250-3300 cm?¹ (N-H/O-H stretching) and 1700-1500 cm?¹ (C=O stretching). SDS-PAGE revealed pure keratin bands (10-15 kDa), while SEM showed layered, porous morphology suitable for biomaterial applications. Thermogravimetric analysis, furthermore, identified three degradation stages occurred at 0-200°C (3.05% loss), 200-400°C (39.37% loss), and 400-700°C (31.13% loss). Amino acid profiling revealed high L-cystine content (153,064.90-156,926.33 mg/kg) with the significant amounts of glycine (63,958.25-64,064.73 mg/kg), L-proline (77,631.16-77,717.42 mg/kg), and L-leucine (59,111.43-59,198.60 mg/kg). In silico molecular docking studies identified leucine as a promising procollagen N-endopeptidase inhibitor (binding energy -5.0 kcal/mol), which controlled the collagen-breaking and forming process. This ability makes keratin potential to be developed as a scaffold for bone tissue regeneration in medical industry.
The Effect of Ultrasonication on the Quality of Keratin Extraction Based on Ionic Liquid from Duck Feather Perdana, Senja Salzanabila Putri; Kusumawati, Nita; Basukiwardojo, Maria Monica Sianita; Setiarso, Pirim; Djalilah, Gina Noor; Rahmawati, Khofifatul
Communications in Science and Technology Vol 10 No 2 (2025)
Publisher : Komunitas Ilmuwan dan Profesional Muslim Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.21924/cst.10.2.2025.1785

Abstract

This study investigates the effect of ultrasonic-assisted extraction (UAE) and solvent extraction (SE) on keratin recovery from duck feathers using sodium sulfide-based ionic liquids under different pH conditions. The results showed that SE at acidic pH (pH=3) achieved the highest yield (92%), whereas UAE showed lower recovery (28%) under mildly acidic conditions (pH=5). Spectroscopic and electrophoretic analyses using FTIR confirmed the β-sheet structure with characteristic peaks at 3400 cm−1 (O–H and N–H stretching) and 1660 cm−1 (C=O stretching). Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis analysis (SDS-PAGE) revealed protein bands in the 15–25 kDa range, typical of β-keratin, with higher intensity in SE. Morphological analysis using SEM revealed finer and more homogeneous particles for UAE, while SE produced denser aggregates. Thermal analysis revealed two main degradation stages, occurring at 0–100 °C and 250–500 °C, with UAE samples exhibiting lower residual mass (5.46%) than SE (8.65%). Particle size analysis showed UAE samples had larger but more uniformly distributed particles. XRD results confirmed semi-crystalline structures, with UAE increasing amorphous content and SE maintaining crystallinity. These findings highlight the complementary advantages for tailoring keratin properties toward diverse applications.