CHARACTERIZATION OF FISH SKIN FROM DEMERSAL SPECIES AS POTENTIAL COLLAGEN SOURCES: KARAKTERISTIK KULIT IKAN DEMERSAL SEBAGAI SUMBER KOLAGEN

Mala Nurilmala; Nurafi Razna Suhaima; Vania Mahardika; Agy Wirabudi Pranata

doi:10.24319/jtpk.17.301-312

Authors

Mala Nurilmala Department of Aquatic Product Technology, Faculty of Fisheries and Marine Science, IPB University, Jl. Agatis, IPB Dramaga Campus, Bogor 16680, Indonesia
Nurafi Razna Suhaima Study Program of Food Quality Assurance Supervisor, School of Vocational Studies, IPB University, Jl. Kumbang No. 14, Bogor 16128, Indonesia
Vania Mahardika Department of Aquatic Product Technology, Faculty of Fisheries and Marine Science, IPB University, Jl. Agatis, IPB Dramaga Campus, Bogor 16680, Indonesia
Agy Wirabudi Pranata PT Geltech Prima Indonesia, Jl. Hanamaru No. 1, Ciapus, Kecamatan Ciomas, Bogor 16610, Indonesia

DOI:

https://doi.org/10.24319/jtpk.17.301-312

Keywords:

amino acids, collagen, demersal fish, fish skin, gelatin

Abstract

The utilization of fishery by-products, particularly fish skin, offers a promising alternative source of halal and safe collagen and gelatin. This study aims to evaluate the characteristics of fish skin from demersal species as potential collagen sources. The fish skins used in this study were from purple-spotted bigeye (Priacanthus tayenus), lattice monocle bream (Scolopsis taenioptera), and Bleeker's grouper (Epinephelus bleekeri). This study employed an experimental and exploratory approach. Analyses included histological observation, proximate composition, amino acid profile, fatty acid profile, and heavy metal content. Histological observations revealed that fish skin was dominated by the dermal layer with well-defined collagen fiber structures, with the thickest collagen layer observed in grouper skin. Proximate analysis indicated that the fish skin samples were characterized by high moisture content (61.05–66.99%) and protein (17.88–20.87%) (wet basis). The amino acid profile showed glycine (3.99% w/w) and alanine (3.15% w/w) as the predominant amino acids, which are characteristic of collagen proteins. Hydroxyproline analysis further confirmed collagen presence, showing an increase from 0.0739 μg/μL in raw skin to 0.4071 μg/μL in gelatin. The fatty acid profile of the mixed sample indicated total detected fatty acid content (55.43% w/w), dominated by saturated fatty acids. Heavy metal analysis showed very low concentration. These findings indicate that fish skin from purple-spotted bigeye, lattice monocle bream, and Bleeker’s grouper has strong potential as an alternative, safe, halal, and value-added source of collagen and gelatin.

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References

Alves AL, Marques ALP, Martins E, Silva TH, Reis RL. 2017. Cosmetic Potential of Marine Fish Skin Collagen. Cosmetics. 4(4): 39. DOI: https://doi.org/10.3390/cosmetics4040039.

[AOAC] Association of Official Analytical Chemists. 2005. Official Methods of Analysis of AOAC International. Gaithersburg (MD): AOAC International.

Atma Y. 2017. Amino Acid and Proximate Composition of Fish Bone Gelatin from Different Warm-water Species: A Comparative Study. The 3rd International Seminar on Sciences "Sciences on Precision and Sustainable Agriculture" (ISS-2016), 4 November 2016, Bogor, Indonesia. IOP Conference Series: Earth and Environmental Science. DOI: https://doi.org/10.1088/1755-1315/58/1/012008.

[BPS] Badan Pusat Statistik. 2024. Buletin Statistik Perdagangan Luar Negeri Impor November 2024. Jakarta (ID): Badan Pusat Statistik.

Chuaychan S, Benjakul S, Nuthong P. 2016. Element Distribution and Morphology of Spotted Golden Goatfish Fish Scales as Affected by Demineralisation. Food Chemistry. 197: 814–820. DOI: https://doi.org/10.1016/j.foodchem.2015.11.044.

Devita L, Nurilmala M, Lioe HN, Suhartono MT. 2021. Chemical and Antioxidant Characteristics of Skin-Derived Collagen Obtained by Acid-Enzymatic Hydrolysis of Bigeye Tuna (Thunnus obesus). Marine Drugs. 19(4): 222. DOI: https://doi.org/10.3390/md19040222.

Dondero L, Atanasio GDN, Tardanico F, Lertora E, Boggia R, Capra V, Cometto A, Costamagna M, Feletti M, Garibaldi F, et al. 2025. Unlocking the Potential of Marine Sidestreams in the Blue Economy: Lessons Learned from the EcoeFISHent Project on Fish Collagen. Marine Biotechnology. 27(63): 1–29. DOI: https://doi.org/10.1007/s10126-025-10438-9.

Ebadi Z, Khodanazary A, Hosseini SM, Zanguee N. 2019. The Shelf Life Extension of Refrigerated Nemipterus japonicus Fillets by Chitosan Coating Incorporated with Propolis Extract. International Journal of Biological Macromolecules. 139: 94–102. DOI: https://doi.org/10.1016/j.ijbiomac.2019.07.204.

Ferreira AM, Gentile P, Chiono V, Ciardelli G. 2012. Collagen for Bone Tissue Regeneration. Acta Biomaterialia. 8(9): 3191–3200. DOI: https://doi.org/10.1016/j.actbio.2012.06.014.

Gomez-Guillen MC, Turnay J, Fernandez Diaz MD, Ulmo N, Lizarbe MA, Montero P. 2002. Structure and Physical Properties of Gelatin Extracted from Different Marine Species: A Comparative Study. Food Hydrocolloids. 16(1): 25–34. DOI: https://doi.org/10.1016/S0268-005X(01)00035-2.

Hadinoto S, Idrus S. 2018. Proporsi dan Kadar Proksimat Bagian Tubuh Ikan Tuna Ekor Kuning (Thunnus albacares) dari Perairan Maluku. Majalah BIAM. 14(2): 51–57.

Haryati D, Nadhira L, Hera H, Abdullah N. 2019. Ekstraksi dan Karakterisasi Gelatin Kulit Ikan Baronang (Siganus canaliculatus) dengan Metode Enzimatis Menggunakan Enzim Bromelin. Canrea Journal. 2(1): 26–31. DOI: https://doi.org/10.20956/canrea.v2i1.177.

Law of the Republic of Indonesia Number 33 of 2014 concerning Halal Product Assurance. Jakarta.

Karim AA, Bhat R. 2009. Fish Gelatin: Properties, Challenges, and Prospects as an Alternative to Mammalian Gelatins. Food Hydrocolloids. 23(3): 563–576. DOI: https://doi.org/10.1016/j.foodhyd.2008.07.002.

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. DOI: https://doi.org/10.1016/j.foodchem.2004.02.042.

[KKP] Kementerian Kelautan dan Perikanan. 2024. Produksi Perikanan. https://portaldata.kkp.go.id. [February 6, 2026].

McGuire M, Beerman KA. 2013. Nutritional Sciences: From Fundamentals to Food. Belmont (CA): Wadsworth Cengage Learning.

Nurilmala M, Pertiwi RM, Nurhayati T, Fauzi S, Batubara I, Ochiai Y. 2019. Characterization of Collagen and its Hydrolysate from Yellowfin Tuna Thunnus albacares Skin and their Potencies as Antioxidant and Antiglycation Agents. Fisheries Science. 85: 591–599. DOI: https://doi.org/10.1007/s12562-019-01303-5.

Nurilmala M, Pratiwi HA, Nugraha R. 2023. Proses Pembuatan Gelatin dari Ikan Patin (IDS000005881). Jakarta (ID): Direktorat Jenderal Kekayaan Intelektual.

Nurilmala M, Sriwahyuni D, Putri EP. 2025. Metode Ekstraksi Gelatin dari Kulit Ikan Patin (IDS000010130). Jakarta (ID): Direktorat Jenderal Kekayaan Intelektual.

Nurilmala M, Suryamarevita H, Hizbullah HH, Jacoeb AM, Ochiai Y. 2022. Fish Skin as a Biomaterial for Halal Collagen and Gelatin. Saudi Journal of Biological Sciences. 29(2): 1100–1110. DOI: https://doi.org/10.1016/j.sjbs.2021.09.056.

Panagan AT, Yohandini H, Wulandari M. 2012. Analisis Kualitatif dan Kuantitatif Asam Lemak Tak Jenuh Omega-3, Omega-6 dan Karakterisasi Minyak Ikan Patin (Pangasius pangasius). Jurnal Penelitian Sains. 15(3): 102–106. DOI: https://doi.org/10.56064/jps.v15i3.105.

Rieuwpassa FJ, Karimela EJ, Lasaru DC. 2018. Karakterisasi Sifat Fungsional Konsentrat Protein Ikan Sunglir (Elagatis bipinnulatus). Jurnal Teknologi Perikanan dan Kelautan. 9(2): 177–183. DOI: https://doi.org/10.24319/jtpk.9.177-183.

Rieuwpassa FJ, Karimela EJ, Karaeng MC. 2020. Analisis Fisiko Kimia Konsentrat Protein Ikan Nila (Oreochromis niloticus) yang Diekstrak Menggunakan Pelarut Etanol. Jurnal Teknologi Perikanan dan Kelautan. 11(1): 45–52. DOI: https://doi.org/10.24319/jtpk.11.45-52.

Rosmawati, Abustam E, Tawali AB, Said MI, Sari DK. 2018. Effect of Body Weight on the Chemical Composition and Collagen Content of Snakehead Fish Channa striata Skin. Fisheries Science. 84: 1081–1089. DOI: https://doi.org/10.1007/s12562-018-1248-8.

Sheehan DC, Hrapchak BB. 1980. Theory and Practice of Histotechnology (2nd ed). St. Louis (US): Mosby.

Statistical Data and Information Center, Ministry of Marine Affairs and Fisheries. 2022. Processing of Marine and Fisheries Production Data. Jakarta (ID): Ministry of Marine Affairs and Fisheries.

Stone RII, Saathoff EC, Larson DA, Wall JT, Wienandt NA, Magnusson S, Kjartansson H, Natesan S, Christy RJ. 2021. Accelerated Wound Closure of Deep Partial Thickness Burns with Acellular Fish Skin Graft. International Journal of Molecular Sciences. 22(4): 1590. DOI: https://doi.org/10.3390/ijms22041590.

Suvik A, Effendy AWM. 2012. The Use of Modified Masson’s Trichrome Staining in Collagen Evaluation in Wound Healing Study. Malaysian Journal of Veterinary Research. 3(1): 39–47.

Wahyuni, Kumorowati E, Pitriani, Achmad H. 2015. Pengembangan Metode Pewarnaan Histologi Khusus Trichrome Masson’s untuk Diagnosa Penyakit pada Hewan. Diagnosa Veteriner. 14(3): 1–5.

Ward AG, Courts A. 1977. The Science and Technology of Gelatin. London (GB): Academic Press.

Waters Corporation. 2012. Acquity UPLC H-Class and H-Class Bio Amino Acid Analysis System Guide. Dublin (IE): Waters Corporation.