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Ionic liquid ultrasound-assisted extraction (IL-UAE) for duck feather keratin and in silico evaluation as a potential procollagen n-endopeptidase inhibitor

Communications in Science and Technology · Vol. 10 No. 1 (2025) · hlm. 75–86

DOI
10.21924/cst.10.1.2025.1669
ISSN
2502-9266, 2502-9258
Terbit
2025-07-31
Penerbit
Komunitas Ilmuwan dan Profesional Muslim Indonesia
Bahasa
eng

Abstrak

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.

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  • Universitas Negeri Surabaya
  • State University of Semarang
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Rekan penulisOrganisasiArtikel bersama
Pirim SetiarsoAfiliasi tidak diketahui14
Supari MuslimAfiliasi tidak diketahui11
Nafisatus ZakiyahAfiliasi tidak diketahui7
Gina Noor DjalilahAfiliasi tidak diketahui5
Senja Salzanabila Putri PerdanaAfiliasi tidak diketahui5
Sinta Anjas CahyaniAfiliasi tidak diketahui4
Samik SamikAfiliasi tidak diketahui4
AR. Sella AuliyaAfiliasi tidak diketahui4
Fadlurachman Faizal FachrirakarsieAfiliasi tidak diketahui3
Amirul Mu'mininAfiliasi tidak diketahui3
Sunu KuntjoroAfiliasi tidak diketahui3
Ita Fatkhur RomadhoniAfiliasi tidak diketahui3
Safira Keysa DewayantiAfiliasi tidak diketahui3
Anandatya Ramdhan Achmad Al ManfalutyAfiliasi tidak diketahui3
Shafira BasriAfiliasi tidak diketahui3
Guntur TrimulyonoAfiliasi tidak diketahui2
Erina RahmadyantiAfiliasi tidak diketahui2
Maria Monica Sianita BasukiwardojoAfiliasi tidak diketahui2
Muhamad Syariffuddien ZuhrieAfiliasi tidak diketahui2
Ahmad Naufal Al HafidlAfiliasi tidak diketahui2
Muchamad Sabilah HanafiAfiliasi tidak diketahui2
Isnawati -Universitas Negeri Surabaya1
Firas KhaleylaAfiliasi tidak diketahui1
Hayu Anggraini Hayu AnggrainiAfiliasi tidak diketahui1
Bambang Tri RahardjoAfiliasi tidak diketahui1
Siti Rasminah ChaelaniAfiliasi tidak diketahui1
Sutiman Bambang SumitroAfiliasi tidak diketahui1
Lisa LisdianaState University of Semarang1
Isnawati IsnawatiAfiliasi tidak diketahui1
Sari Edi CahyaningrumAfiliasi tidak diketahui1

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Sumber metadata: OAI-PMH (metadata jurnal) https://cst.kipmi.or.id/oai, pertama di-harvest 8 Nov 2026, terakhir terlihat 8 Nov 2026.
Metadata asli (oai_dc) 
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	<dc:title xml:lang="en-US">Ionic liquid ultrasound-assisted extraction (IL-UAE) for duck feather keratin and in silico evaluation as a potential procollagen n-endopeptidase inhibitor</dc:title>
	<dc:creator>Sianita, Maria Monica</dc:creator>
	<dc:creator>Kusumawati, Nita</dc:creator>
	<dc:creator>Asri, Mahanani Tri</dc:creator>
	<dc:creator>Dzulkarnain, Shod Abdurrachman</dc:creator>
	<dc:creator>Al Hafidl, Achmad Naufal</dc:creator>
	<dc:creator>Kahfi, Ashabul</dc:creator>
	<dc:creator>Nabila, Mutiara Azfa</dc:creator>
	<dc:creator>Setiawan, Ferdiansyah</dc:creator>
	<dc:creator>Isyrak, Luthfiyah</dc:creator>
	<dc:creator>Rahmawati, Khofifatul</dc:creator>
	<dc:subject xml:lang="en-US">Keratin</dc:subject>
	<dc:subject xml:lang="en-US">Duck feathers</dc:subject>
	<dc:subject xml:lang="en-US">Ionic liquid</dc:subject>
	<dc:subject xml:lang="en-US">Ultrasound-Assisted Extraction</dc:subject>
	<dc:subject xml:lang="en-US">Procollagen N-Endopeptidase Inhibitor</dc:subject>
	<dc:description xml:lang="en-US">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.</dc:description>
	<dc:publisher xml:lang="en-US">Komunitas Ilmuwan dan Profesional Muslim Indonesia</dc:publisher>
	<dc:date>2025-07-31</dc:date>
	<dc:type>info:eu-repo/semantics/article</dc:type>
	<dc:type>info:eu-repo/semantics/publishedVersion</dc:type>
	<dc:format>application/pdf</dc:format>
	<dc:identifier>https://cst.kipmi.or.id/journal/article/view/1669</dc:identifier>
	<dc:identifier>10.21924/cst.10.1.2025.1669</dc:identifier>
	<dc:source xml:lang="en-US">Communications in Science and Technology; Vol. 10 No. 1 (2025); 75-86</dc:source>
	<dc:source xml:lang="id-ID">Communications in Science and Technology; Vol 10 No 1 (2025); 75-86</dc:source>
	<dc:source>2502-9266</dc:source>
	<dc:source>2502-9258</dc:source>
	<dc:source>10.21924/cst.10.1.2025</dc:source>
	<dc:language>eng</dc:language>
	<dc:relation>https://cst.kipmi.or.id/journal/article/view/1669/212</dc:relation>
	<dc:rights xml:lang="en-US">Copyright (c) 2025 Communications in Science and Technology</dc:rights>
</oai_dc:dc>