Giavy, Salsabila (2025) Analisis Pengaruh Konsentrasi Papain dan Waktu Perendaman Terhadap Karakteristik Kolagen dari Kulit Ikan Kuniran (Upeneus sulphureus). Other thesis, Institut Teknologi Sepuluh Nopember.
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Abstract
Kolagen merupakan protein struktural utama yang banyak dimanfaatkan dalam bidang biomedis karena sifatnya yang biokompatibel dan biodegradabel. Seiring meningkatnya kebutuhan kolagen dari sumber nonmamalia, pencarian bahan baku alternatif menjadi penting guna menghindari isu religius, etis, serta risiko zoonosis. Kulit ikan kuniran (Upeneus sulphureus) memiliki potensi sebagai sumber kolagen alternatif yang belum banyak dimanfaatkan dan relatif mudah diperoleh. Penelitian ini bertujuan untuk menganalisis pengaruh variasi konsentrasi enzim papain (0,5%, 1%, dan 1,5%) serta waktu perendaman (24, 48, dan 72 jam) terhadap karakteristik kolagen hasil ekstraksi enzimatik. Hasil menunjukkan bahwa waktu perendaman memberikan pengaruh signifikan terhadap rendemen, dengan hasil tertinggi sebesar 8,88% pada perendaman 48 jam menggunakan papain 0,5%. Semakin lama waktu perendaman dan semakin tinggi konsentrasi papain yang digunakan, nilai pH cenderung menurun, yakni berkisar antara 2,81–3,20. Kadar air dan kadar abu yang diperoleh berkisar antara 7,4–14,8% dan 4,15%–7,52%. Spektrum FTIR menunjukkan keberadaan gugus amida A, B, I, II, dan III yang menandakan struktur triple helix kolagen masih terjaga. Hasil DSC menunjukkan bahwa peningkatan konsentrasi papain dapat meningkatkan stabilitas termal kolagen, dengan suhu denaturasi (Tmax) tertinggi sebesar 204,45 °C pada sampel dengan papain 1,5% selama 48 jam. Dengan karakteristik tersebut, kulit ikan kuniran hasil ekstraksi enzimatik menunjukkan potensi besar untuk dikembangkan sebagai bahan baku kolagen, seperti aplikasi medis.
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Collagen is a major structural protein extensively utilized in the biomedical field due to its biocompatibility and biodegradability. In response to the growing demand for collagen from nonmammalian sources, the exploration of alternative raw materials has become increasingly important to address religious, ethical, and zoonotic concerns. The skin of sulphur goatfish (Upeneus sulphureus) represents a promising yet underexplored source of collagen that is relatively accessible. This study aimed to evaluate the effect of varying papain enzyme concentrations (0.5%, 1%, and 1.5%) and soaking durations (24, 48, and 72 hours) on the characteristics of collagen extracted enzymatically from Upeneus sulphureus skin. The results showed that soaking time significantly influenced yield, with the highest yield (8.88%) obtained at 48 hours using 0.5% papain. Increasing soaking time and enzyme concentration tended to decrease the pH of the collagen solution, ranging from 2.81 to 3.20. The moisture content ranged from 7.4% to 14.8%, while ash content ranged from 4.15% to 7.52%. FTIR analysis confirmed the presence of characteristic amide bands (A, B, I, II, and III), indicating the preservation of the collagen triple helix structure. Furthermore, DSC analysis revealed that higher papain concentrations enhanced the thermal stability of collagen, with the highest denaturation temperature (Tmax) observed at 204.45 °C in the sample treated with 1.5% papain for 48 hours. These findings suggest that enzymatically extracted collagen from Upeneus sulphureus skin exhibits favorable physicochemical properties, demonstrating its potential as a sustainable and functional collagen source for biomedical applications.
Item Type: | Thesis (Other) |
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Uncontrolled Keywords: | Ikan Kuniran, Kolagen, Papain, PaSC Collagen, Sulphur Goatfish, Papain, PaSC |
Subjects: | T Technology > TP Chemical technology > TP1140 Polymers T Technology > TP Chemical technology > TP156 Crystallization. Extraction (Chemistry). Fermentation. Distillation. Emulsions. T Technology > TP Chemical technology > TP248.65.P76 Proteins--Biotechnology. |
Divisions: | Faculty of Industrial Technology and Systems Engineering (INDSYS) > Material & Metallurgical Engineering > 28201-(S1) Undergraduate Thesis |
Depositing User: | Salsabila Giavy |
Date Deposited: | 01 Aug 2025 02:03 |
Last Modified: | 01 Aug 2025 02:03 |
URI: | http://repository.its.ac.id/id/eprint/124504 |
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