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)

Aula Sakinah, Wini Trilaksani, Tati Nurhayati


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.


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Aula Sakinah
aulasakinah@apps.ipb.ac.id (Primary Contact)
Wini Trilaksani
Tati Nurhayati
SakinahA., TrilaksaniW., & NurhayatiT. (2023). 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). Jurnal Pengolahan Hasil Perikanan Indonesia, 26(3). https://doi.org/10.17844/jphpi.v26i3.45529

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