Karakteristik papain soluble collagen gelembung renang ikan manyung dengan variasi praperlakuan alkali dan rasio ekstraktan Characterization of papain-soluble collagen from swim bladder sea catfish with variations in alkali pretreatment and extractant ratio
Article Sidebar
Accepted
15 February 2024
Published
7 March 2024
Keywords:
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acetic acid, enzyme, extraction, fish collagen, yield
Abstract
Collagen is a crucial biomaterial in multiple sectors of Indonesia, yet its procurement remains heavily reliant on imports. Catfish swim bladders are considered valuable sources of collagen. It is crucial to optimize the extraction process to obtain a higher yield, which is influenced by variables such as the pretreatment time and sample-to-extractant ratio. This study aimed to maximize the duration of alkali soaking and investigate the influence of various alkali types and extractant-to-sample ratios on collagen extraction from sea catfish swim bladders. This study was comprised of two phases. The first phase involved determining the optimal soaking time in an alkaline solution (KOH). The second phase involved papain-soluble collagen extraction for 48 h, with variations in alkali (KOH and NaOH 0.05 M) and sample-to-extractant ratios (1:10, 1:20, 1:30, w/v). Papain enzyme at 5,000 U/g in 0.5 M acetic acid was utilized as the extractant. The parameters analyzed included fish proportion, proximate amino acids, protein concentration, yield, thermal stability, functional groups, molecular weight, and zeta potential. The data indicate that the sea catfish swim bladder possesses a percentage of 4.08%, and its protein content is 33.58±0.11%. The bladder contains characteristic amino acids, such as proline (29.2 mg/g), alanine (28.9 mg/g), and hydroxyproline (18.18 mg/g). The most suitable duration for alkali soaking using potassium hydroxide (KOH) was determined to be 6 h. Furthermore, the most effective method for extracting papain-soluble collagen involved alkali pretreatment using sodium hydroxide (NaOH) for 6 h with a sample extractant ratio of 1:20 (w/v). The yield of collagen obtained was 35.31±0.65%, which displayed characteristic amide groups (A, B, I, II, and III), an electrophoresis pattern consisting of α1, α2, and β, a maximum transition temperature of 33.06°C, and a zeta potential of +32 mV.
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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:10.1016/j.jmbbm.2018.06.021
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Idrus, S., Hadinoto, S., & Kolanus, J. (2018). karakterisasi kolagen gelembung renang tuna sirip kuning (Thunnus albacares) dari perairan maluku menggunakan ekstraksi asam. Biopropal Ind, 9(2), 87-94. https://doi.org/10.36974/jbi.v9i2.4020
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Jaswir, I., Monsur, H.A., & Salleh, H.M. (2011). Nano-structural analysis of fish collagen extracts for new process development. African Journal Biotechnology, 10(81), 18847-18854. https://doi.org/10.5897/AJB11.2764
Kaewdang, O., Benjakul, S., Kaewmanee, T., & Kishimura, H. (2014). Characteristics of collagens from the swim bladders of yellowfin tuna (Thunnus albacares). Food Chemical, 155, 264–270. https://doi.org/10.1016/j.foodchem.2014.01.076
Kiew, P. L., & Mat Don, M. (2012). Collagen extraction from Malaysian cultured catfish (hybrid Clarias sp.): kinetics and optimization of extraction conditions using response surface methodology. International Scholarly Research Notices.
Kartika, I. W. D., Trilaksani, W., Adnyane, I. K. M. (2016). Karakterisasi kolagen limbah gelembung renang ikan cunang hasil ekstraksi asam dan hidrotermal. Journal Pengolahan Hasil Perikanan Indonesia, 19(3), 222-232. https://doi.org/10.17844/jphpi.2016.19.3.222
Kirkness, M.W., Lehmann, K., & Forde, N. R. (2019). Mechanics and structural stability of the collagen triple helix. Journal Current Opinion in Chemical Biology, 53(4), 98-105. https://doi.org/10.1016/j.cbpa.2019.08.001
Kittiphatanabawon, P., Benjakul, S., Visessanguan, W., Nagai, T., & Tanaka, M. (2005). Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus). Journal Food Chemical, 89(3), 363-373. 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
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 Science Food Agriculture, 97(5), 1451-1458. https://doi.org/10.1002/jsfa.7884
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 38 (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 Chemical, 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 Chemical, 172, 836-843. https://doi.org/10.1016/j.foodchem.2014.09.147
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Authors
UtamiR., TrilaksaniW., & HardiningtyasS. D. (2024). Karakteristik papain soluble collagen gelembung renang ikan manyung dengan variasi praperlakuan alkali dan rasio ekstraktan: Characterization of papain-soluble collagen from swim bladder sea catfish with variations in alkali pretreatment and extractant ratio . Jurnal Pengolahan Hasil Perikanan Indonesia, 27(3), 223-241. https://doi.org/10.17844/jphpi.v27i3.49968
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