Peningkatan Kualitas Fisik dan Kimia Papain Soluble Collagen Kulit Ikan Nila dengan Variasi Waktu Ultrasound-Assisted Pre-Treatment

Abstract

Berbagai jenis dan bagian biota perairan, termasuk kulit ikan nila berpotensi sebagai sumber material kolagen, namun rendemen dan metode ekstraksinya masih perlu dioptimalkan. Penggunaan ultrasound-assisted pre-treatment dapat mempercepat proses, meningkatkan rendemen, serta menghasilkan mutu kolagen yang baik. Penelitian bertujuan untuk menentukan pengaruh ultrasound-assisted pre-treatment dalam meningkatkan rendemen dan mempertahankan karakteristik papain soluble collagen kulit ikan nila. Praperlakuan dilakukan dengan variasi waktu ultrasonikasi selama 0, 90, dan 150 menit yang dikombinasikan dengan perendaman dalam larutan NaOH 0,1M selama 12 jam. Hasil menunjukkan ultrasonikasi 150 menit dan perendaman dalam larutan NaOH selama 8 jam mampu meningkatkan rendemen kolagen dari 18,68±0,47% hingga 29,41±0,44%. Kandungan protein non-kolagen direduksi hingga mencapai 0,52 mg/mL. Metode ini mampu meningkatkan kandungan hidroksiprolin (1,83 menjadi 62,06mg/g) dan rasio Hyp/Protein (3,56 menjadi 10,69%). Rasio Hyp/Imono acid mencapai 42,21% dan faktor konversi terhadap kolagen yaitu 10,2. Analisis bobot molekul dan gugus fungsi mengindikasikan kolagen kulit ikan nila memiliki rantai a dan ß serta puncak pita amida sebagai kolagen tipe I.

Various aquatic organisms and their body parts, including Nile tilapia (Oreochromis niloticus) skin, had potential to serve as sources of collagen material; however, the yield and extraction methods still required optimization. The use of ultrasound-assisted pre-treatment had the potential to accelerate the extraction process, enhance yield, and improve the quality of the resulting collagen. This study aimed to determine the effect of ultrasound-assisted pre-treatment on increasing the yield and preserving the characteristics of papain-soluble collagen derived from Nile tilapia skin. The pre-treatment was conducted using ultrasonic durations of 0, 90, and 150 minutes, combined with immersion in 0.1 M NaOH solution for 12 hours. The results showed that 150 minutes of ultrasonication followed by 8 hours of NaOH treatment increased the collagen yield from 18.68?±?0.47% to 29.41?±?0.44%. The non-collagenous protein content was reduced to 0.52 mg/mL. This method significantly increased the hydroxyproline content (from 1.83 to 62.06 mg/g) and the Hyp/Protein ratio (from 3.56% to 10.69%). The Hyp/Imono acid ratio reached 42.21%, and the conversion factor to collagen was 10.2. Molecular weight and functional group analysis indicated the presence of a and ß chains, along with distinct amide band peaks, confirming the collagen as type I.