Ekstraksi dan determinasi karakteristik kolagen gelembung renang ikan lencam (Lethrinus lentjan): Extraction and determination characteristics of swim bladder collagen in pink ear emperor fish (Lethrinus lentjan)

Ekspor filet ikan lencam yang terus meningkat di Indonesia menyebabkan peningkatan pada jumlah hasil samping produksi, salah satunya gelembung renang. Gelembung renang ikan merupakan sumber alternatif kolagen yang telah menarik minat ilmuwan dan industri untuk diaplikasikan di berbagai sektor kesehatan, farmasi, dan kosmetik. Penelitian ini bertujuan untuk menentukan rasio bahan dan pelarut serta waktu yang optimal pada tahap praperlakuan dalam ekstraksi kolagen dari gelembung renang ikan lencam. Penelitian dibagi menjadi tiga tahapan, yaitu optimasi praperlakuan sampel menggunakan larutan NaOH dengan lama waktu yang berbeda, ekstraksi dengan rasio bahan dan pelarut asam asetat dan penambahan enzim papain, dan karakterisasi kolagen gelembung renang ikan lencam. Analisis komponen gelembung renang ikan lencam meliputi proksimat, asam amino, dan protein terlarut. Analisis kualitas kolagen meliputi proksimat, asam amino, pengukuran warna, derajat putih, pH, pita protein, dan gugus fungsi. Kondisi praperlakuan terbaik didapat pada gelembung renang ikan lencam yang direndam NaOH 0,1 M selama 8 jam. Ekstrasi kolagen gelembung renang ikan lencam terbaik, yaitu rasio 1:30 (b/v) larut enzim papain (PaSC) sebesar 28,88±0,71% selama 48 jam. Kandungan protein mencapai 92,56±0,12%, derajat putih 97,86%, nilai pH 6,64, kandungan hidroksiprolina sebesar 79,32 mg/g, glisina 293,35 mg/g, dan prolina 102,57 mg/g sebagai asam amino penciri kolagen. Hasil deteksi gugus fungsi menunjukkan adanya gugus fungsi amida I, II, III, A, dan B serta rantai α1 dan α2 . Pola protein kolagen terdeteksi pada kisaran molekul 100-250 kDa yang mengindikasikan kolagen tipe I.The upswing in the exportation of Lethrinus lentjan fillets in Indonesia has resulted in a concomitant increase in the quantity of production by-products, including swim bladder. Fish swim bladders possess collagen, which has garnered interest from both the scientific and industrial communities for potential applications in healthcare, pharmaceuticals, and cosmetics. The primary objective of this study was to ascertain the most suitable ratio of materials and solvents, as well as the optimal duration of pretreatment, for the effective extraction of collagen from the swim bladders of pink ear emperor fish. The study was conducted in three distinct stages: pretreatment of the sample with NaOH solutions of varying durations, extraction of collagen using papain enzyme and varying ratios of materials and acetic acid, and characterization of the extracted collagen. Examination of the swim bladder constituents of pink ear emperor fish encompasses proximate, amino acid, and dissolved protein analyses. Quality analysis of collagen encompasses various techniques, including proximate analysis, amino acid analysis, color measurement, whiteness degree assessment, pH determination, protein band analysis, and functional group detection. These methods are used to evaluate the chemical and physical properties of collagen, ensuring its purity and suitability for various applications. The optimal pretreatment conditions involved soaking pink ear emperor fish swim bladders in 0.1 M NaOH for 8 h, and the highest yield of collagen was attained using a soluble papain enzyme ratio of 1:30 (w/v) for 48 h, resulting in a collagen output of 28.88±0.71%.The extracted collagen possessed a protein content of 92.56±0.12%, a whiteness degree of 97.86%, a pH value of 6.64, a hydroxyproline content of 79.32 mg/g, a glycine content of 293.35 mg/g, and a proline content of 102.57 mg/g. These values are characteristic of the amino acids found in collagen. The results of functional group detection experimentally confirmed the presence of amide I, II, III, A, and B functional groups, as well as α1 and α2 chains. Collagen protein band analysis identified the presence of collagen type I in the molecular range of 100-250 kDa, as evidenced by the detection of collagen protein patterns in this range