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)
Article Sidebar
Accepted
2 June 2023
Published
17 November 2023
Keywords:
-
characterization, collagen, extraction, fish swim bladder, yield
Abstract
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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Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem, 72(1-2), 248-254. https://doi.org/10.1016/0003- 2697(76)90527-3.
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Bielajew, B. J., Hu, J. C., & Athanasiou, K. A. (2020). Collagen: quantification, biomechanics and role of minor subtypes in cartilage. Nature Review Materials. 1–18
Chen, J., Li, L., Yi, R., Xu, N., Gao, R., & Hong, B. (2016). Extraction and characterization of acid-soluble collagen from scales and skin of tilapia (Oreochromis niloticus). Lwt, 66, 453–459. https://doi.org/10.1016/j.lwt.2015.10.070.
Chen, Y., Jin, H., Yang, F., Jin, S., Liu, C., Zhang, L., Huang, J., Wang, S., Yan, Z., Cai, X., Zhao, R., Yu, F., Yang, Z., Ding, G., & Tang, Y. (2019). Physicochemical, antioxidant properties of giant croaker (Nibea japonica) swim bladders collagen and wound healing evaluation. International Journal of Biological Macromolecules, 138, 483–491. https://doi.org/10.1016/j.ijbiomac.2019.07.111.
Cherim M, Mustafa A, Cadar E, Lupașcu N, Paris S, Sirbu R. (2016). Collagen Sources and Areas of Use. Europe Journal Interdiscip Study. 4(1):122. doi:10.26417/ejis.v4i1.p122-128.
Coppola, D., Lauritano, C., Esposito, F. P., Riccio, G., Rizzo, C., & de Pascale, D. (2021). Fish waste: from problem to valuable resource. Marine Drugs, 19(2), 1–39. https://doi.org/10.3390/MD19020116.
Djailani, F., Trilaksani, W., & Nurhayati, T. (2016). Optimasi ekstraksi dan karakterisasi kolagen dari gelembung renang ikan cunang dengan metode asam-hidro- ekstraksi. Journal Pengolahan Hasil Perikanan Indonesia, 19(2), 156–167. https://doi.org/10.17844/jphpi.2019.19.2.156.
Gadi, S. D. (2017). Kolagen larut asam dari gelembung renang Ikan cunang (Muarenesox talabon) sebagai sediaan krim pelembab wajah [Tesis]. Institut Pertanian Bogor.
Gaurav, Kumar, P., Nidheesh, T., Govindaraju, K., Jyoti, & Suresh, P. V. (2017). Enzymatic extraction and characterisation of a thermostable collagen from swim bladder of rohu (Labeo rohita). Journal of the Science of Food and Agriculture, 97(5), 1451–1458. https://doi.org/10.1002/jsfa.7884.
Ghanaeian, A., & Soheilifard, R. (2018). Mechanical elasticity of proline-rich and hydroxyproline-rich collagen-like triple-helices studied using steered molecular dynamics. Journal of the Mechanical Behavior of Biomedical Materials, 86, 105–112. https://doi.org/10.1016/j.jmbbm.2018.06.021.
Grzonka, Z., Kasprzykowski, F., & Wiczk. (2007). Cysteine Proteases. Industrial Enzymes: Structure, Function and Application. Springer.
Jafari, H., Lista, A., Siekapen, M. M., Ghaffari-Bohlouli, P., Nie, L., Alimoradi, H., & Shavandi, A. (2020). Fish collagen: extraction, characterization, and applications for biomaterials engineering. Polymers (Basel), 12(10), 1–37. https://doi.org/10.3390/polym12102230.
Jamilah, B., Umi Hartina, M. R., Mat Hashim, D., & Sazili, A. Q. (2013). Properties of collagen from barramundi (Lates calcarifer) skin. International Food Research Journal, 20(2), 791–798.
Kaewdang, O., Benjakul, S., Kaewmanee, T., & Kishimura, H. (2014). Characteristics of collagens from the swim bladders of yellowfin tuna (Thunnus albacares). Food Chemistry, 155, 264–270. https://doi.org/10.1016/j.foodchem.2014.01.076.
Kartika, I. W. D., Trilaksani, W., & Adnyane, I. K. M. (2016). Karakterisasi kolagen limbah gelembung renang ikan cunang hasil ekstraksi asam dan hidrotermal. Jurnal Pengolahan Hasil Perikanan Indonesia, 19(3), 222–232. https://doi.org/10.17844/jphpi.2016.19.3.222.
Kementerian Kelautan dan Perikanan. (2018). Produksi Perikanan. Pusat Data Statistik dan Informasi Kementerian Kelautan dan Perikanan.
Kementerian Kelautan dan Perikanan. (2021). Produksi perikanan tangkap laut jenis ikan tuna. Statistik KKP. https://statistik.kkp.go.id/home.php?.m=total&i=2#panel-footer.
Kittiphattanabawon, P., Benjakul, S., Visessanguan, W., Nagai, T., & Tanaka, M. (2005). Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus). Food Chemistry, 89(3), 363–372. https://doi.org/10.1016/j.foodchem.2004.02.042.
Kong, J., & Yu, S. (2007). Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochimica et Biophysica Sinica, 39(8), 549–559. https://doi.org/10.1111/j.1745-7270.2007.00320.x.
Laemmli, U. K. (1970). Cleavage of structural protein during the assembly of head of bacteriophage T4. Nature, 277(5259), 680-685.
Li, J., Li, Y., Li, Y., Yang, Z., & Jin, H. (2020). Physicochemical properties of collagen from acaudina molpadioides and its protective effects against H2O2-induced injury in RAW264.7 cells. Marine Drugs, 18(7). https://doi.org/10.3390/MD18070370.
Lin, F., Rong, H., Lin, J., Yuan, Y., Yu, J., Yu, C., You, C., Wang, S., Sun, Z., & Wen, X. (2020). Enhancement of collagen deposition in swim bladder of Chu’s croaker (Nibea coibor) by proline: View from in-vitro and in-vivo study. Aquaculture, 523, 735175. https://doi.org/10.1016/j.aquaculture.2020.735175.
Liu, D., Liang, L., Regenstein, J. M., & Zhou, P. (2012). Extraction and characterisation of pepsin-solubilised collagen from fins, scales, skins, bones and swim bladders of bighead carp (Hypophthalmichthys nobilis). Food Chemistry, 133(4), 1441–1448. https://doi.org/10.1016/j.foodchem.2012.02.032.
Liu, D., Wei, G., Li, T., Hu, J., Lu, N., Regenstein, J. M., & Zhou, P. (2015). Effects of alkaline pretreatments and acid extraction conditions on the acid-soluble collagen from grass carp (Ctenopharyngodon idella) skin. Food Chemistry, 172, 836–843. https://doi.org/10.1016/j.foodchem.2014.09.147.
Mattjik AA, Sumertajaya M. (2002). Perancangan Percobaan dengan Aplikasi SAS dan Minitab. Bogor (ID) :IPB Press.
Meng, D., Tanaka, H., Kobayashi, T., Hatayama, H., Zhang, X., Ura, K., Yunoki, S., & Takagi, Y. (2019). The effect of alkaline pretreatment on the biochemical characteristics and fibril-forming abilities of types I and II collagen extracted from bester sturgeon by-products. International Journal of Biological Macromolecules, 131, 572–580. https://doi.org/10.1016/j.ijbiomac.2019.03.091.
Nilsuwan, K., Fusang, K., Pripatnanont, P., & Benjakul, S. (2022). Properties and characteristics of acid-soluble collagen from salmon skin defatted with the aid of ultrasonication. Fishes. 7(1), 1–14. https://doi.org/10.3390/fishes7010051.
Nollet, L. M. L. (1996). Handbook of food analysis: physical characterization dan nutrient analysis. Edisi ke-2. CRC Press LLC.
Pal, G. K., Nidheesh, T., & Suresh, P. V. (2015). Comparative study on characteristics and in vitro fibril formation ability of acid and pepsin soluble collagen from the skin of catla (Catla catla) and rohu (Labeo rohita). Food Research International, 76, 804–812. https://doi.org/10.1016/j.foodres.2015.07.018.
Romadhon, R., Darmanto, Y. S., & Kurniasih, R. A. (2019). The difference characteristics of collagen from tilapia (Oreochromis niloticus) bone, skin, and scales. Jurnal Pengolahan Hasil Perikanan Indonesia, 22(2), 403–410. https://doi.org/10.17844/jphpi.v22i2.28832.
Safithri, M., Tarman, K., Suptijah, P., & Widowati, N. (2019). Karakteristik fisikokimia kolagen larut asam dari kulit ikan parang-parang (Chirocentrus dorab). Jurnal Pengolahan Hasil Perikanan Indonesia, 22(3), 441-452. https://doi.org/10.17844/jphpi.v22i3.28924.
Schmidt, M. M., Dornelles, R. C. P., Mello, R. O., Kubota, E. H., Mazutti, M. A., Kempka, A. P., & Demiate, I. M. (2016). Collagen extraction process. International Food Research Journal, 23(3), 913-922.
Silva, R. S. G., Bandeira, S. F., & Pinto, L. A. A. (2014). Characteristics and chemical composition of skins gelatin from cobia (Rachycentron canadum). LWT - Food Science and Technology, 57(2), 580–585. https://doi.org/10.1016/j.lwt.2014.02.026.
Simamora, G. R. R., Trilaksani, W., & Uju. (2019). Profiling kolagen gelembung renang ikan patin (Pangasius sp.) melalui proses enzimatis. Jurnal Pengolahan Hasil Perikanan, 2(22), 299-310. https://doi.org/10.17844/jphpi.v22i2.27717.
Singh, P., Benjakul, S., Maqsood, S., & Kishimura, H. (2011). Isolation and characterisation of collagen extracted from the skin of striped catfish (Pangasianodon hypophthalmus). Food Chemistry, 124(1), 97–105. https://doi.org/10.1016/j.foodchem.2010.05.111.
Singh, P., Benjakul, S., Maqsood, S., & Kishimura, H. (2011). Isolation and characterisation of collagen extracted from the skin of striped catfish (Pangasianodon hypophthalmus). Food Chemistry, 124, 97-105.
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Authors
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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