ISSN 2074-9414 (Print),
ISSN 2313-1748 (Online)

Physicochemical and Biotechnological Properties of Marine Collagen Materials

How to quote?
Kulikova YuV, Sporysheva DI, Tashkinov MA, Noskova SYu, Babich OO. Physicochemical and Biotechnological Properties of Marine Collagen Materials. Food Processing: Techniques and Technology. 2026;56(1):190–202. (In Russ.) https://doi.org/10.21603/2074-9414-2026-1-2632 
About journal
Funding
The research was supported by the Ministry of Science and Higher Education of the Russian Federation, contract no. 075-15-2023-601 (13.2251.21.0219).
Abstract
As the current agricultural production capacity fails to meet the growing demand for meat products, the global market might soon face meat shortages. Cultured, or cultivated, meat is a prospective solution to protein security challenges. Its bioproduction relies on a three-dimensional scaffold that defines the structural and mechanical properties of the final product. The food science is seeking new scaffolding materials that would yield cultured meat with targeted sensory and textural properties. This article describes the physical and chemical properties of marine collagen to evaluate its biotechnological potential as raw material for cultured meat scaffolds.
The study investigated collagen derived from jellyfish (Aurelia aurita) and zander skin (Sander lucioperca) obtained by acid extraction. The physicochemical characterization involved the Laemmli electrophoretic method, capillary electrophoresis, FTIR spectroscopy, MTT assay, and 3D bioprinting.
The collagen consisted of two polypeptide chains (α and β) with molecular weights of 240 kDa (A. aurita) and 220 kDa (S. lucioperca). The samples exhibited an optimal isoelectric point, which supported cell culture growth and development. Hydroxyproline, glycine, and proline provided molecules with robust scaffolding properties. The marine collagen demonstrated biocompatibility but no cytotoxicity.
The collagen samples from A. aurita biomass and S. lucioperca skin demonstrated good prospects as biomaterial for scaffolds in cultured meat production.
Keywords
Collagen, marine collagen, biomaterial, scaffold, cultured meat, Aurelia aurita, Sander lucioperca, biocompatibility, MTT analysis
References
  1. Gu H, Kong Y, Huang D, Wang Y, Raghavan V, et al. Scaling cultured meat: Challenges and solutions for affordable mass production. Comprehensive Reviews in Food Science and Food Safety. 2025;24(4):e70221. https://doi.org/10.1111/1541-4337.70221
  2. Gu Y, Li X, Chan ECY. Risk assessment of cultured meat. Trends in Food Science & Technology. 2023;138:491–499. https://doi.org/10.1016/j.tifs.2023.06.037
  3. Berners-Lee M, Kennelly C, Watson R, Hewitt CN. Current global food production is sufficient to meet human nutritional needs in 2050 provided there is radical societal adaptation. Elementa: Science of the Anthropocene. 2018;6(1):52. https://doi.org/10.1525/elementa.310
  4. Park SM, Ryoo JH, Kwon HC, HanSG. Scaffold biomaterials in the development of cultured meat: A review. Food Science of Animal Resources. 2025;45(3):688–710. https://doi.org/10.5851/kosfa.2025.e13
  5. Post MJ, Levenberg S, Kaplan DL, Genovese N, Fu J, et al. Scientific, sustainability and regulatory challenges of cultured meat. Nature Food. 2020;1(7):403–415. https://doi.org/10.1038/s43016-020-0112-z
  6. Xu Y, Liu D, Zhang X, Yang J, Cao J, et al. Functionalized gelatin‐based materials: Advancing bio‐fabrication applications for cell‐cultured meat. Comprehensive Reviews in Food Science and Food Safety. 2025;24(6):70306. https://doi.org/10.1111/1541-4337.70306
  7. Jung S, Choi B, Lee M, Park S, Choi W, et al Bio-orchestration of cellular organization and human-preferred sensory texture in cultured meat. ACS nano. 2025;19(2):2809–2821. https://doi.org/10.1021/acsnano.4c15622
  8. Bomkamp C, Skaalure SC, Fernando GF, Ben-Arye T, Swartz EW, et al. Scaffolding biomaterials for 3D cultivated meat: prospects and challenges. Advanced Science. 2022;9(3):2102908. https://doi.org/10.1002/advs.202102908
  9. Imran M, Liyan Z. Production of plant-based meat: functionality, limitations and future prospects. Food Research and Technology. 2023;249(9):2189– 2213. https://doi.org/10.1007/s00217-023-04287-w
  10. Kulikova Yu, Sukhikh S, Zhikhreva A, Noskova S, Babich O. Comparative analysis of collagen from different sources for wound and burn management. BMT. 2025;00013. https://doi.org/10.12336/bmt.25.00013
  11. Socrates R, Nagarajan S, Bechelany M, Kalkura N. Collagen based biomaterials for tissue engineering applications: A review. Processes and Phenomena on the Boundary Between Biogenic and Abiogenic Nature. 2019;3–22. https://doi.org/10.1007/978-3-030-21614-6_1
  12. Amirrah IN, Lokanathan Y, Zulkiflee I, Wee MMR, Motta A, et al. A comprehensive review on collagen type I development of biomaterials for tissue engineering: From biosynthesis to bioscaffold. Biomedicines. 2022;10(9):2307. https://doi.org/10.3390/biomedicines10092307
  13. Cen L, Liu W, Cui L, Zhang W, Cao Y. Collagen tissue engineering: development of novel biomaterials and applications. Pediatric research. 2008;63(5):492–496. https://doi.org/10.1203/pdr.0b013e31816c5bc3
  14. Kozik W, Polak-Bielawska D, Kutaj A, Savitskaya T. Collagen as a bioactive ingredient in nutricosmetology – a review. Quality in Sport. 2025;46:66618–66618. https://doi.org/10.12775/QS.2025.46.66618
  15. Ferreira AM, Gentile P, Chiono V, Ciardelli G. Collagen for bone tissue regeneration.Acta Biomaterialia. 2012;8(9):3191–3200. https://doi.org/10.1016/j.actbio.2012.06.014
  16. Bronzino J. The biomedical engineering handbook. Boca Raton: CRC Press; 2000. 3189 p.
  17. Ezati P, Khan A, Bhattacharya T, Zaitoon A, Zhang W, et al. Recent Advances in collagen and collagen-based packaging materials: A review. ACS Food Science & Technology. 2025;5(5):1767–1784. https://doi.org/10.1021/acsfoodscitech.4c00938
  18. Barzideh Z, Latiff AA, Gan CY, Benjakul S, Karim AA. Isolation and characterisation of collagen from the Ribbon jellyfish (Chrysaora sp.). International Journal of Food Science and Technology. 2014;49(6):1490–1499. https://doi.org/10.1111/ijfs.12464
  19. Nashchekina YA, Sirotkina MY, Darvish DM, Barsuk IA, Moskalyuk OA, et al. The effect of carbodiimide on the structural, mechanical and biological properties of collagen films. Cell and Tissue Biology. 2021;15(6):586–593. https://doi.org/10.1134/S1990519X21060079
  20. Rangel-Garcia AM, Alvarez-Perez MA, Rivera-Torres F, Piña-Barba MC. Study of the effect of two different chemical cross-linking agents (EDC/NHS and genipin) on the physical, chemical, and mechanical properties of collagen, polycaprolactone, and chitosan scaffolds. Biomedical Materials & Devices. 2025;3:1491–1500. https://doi.org/10.1134/S1990519X21060079
  21. Kargin V. A., Slonimsky G. L. Brief essays on the physical chemistry of polymers. Moscow: Khimia; 1967. 232 p. (In Russ.)
  22. Ahmad M, Benjakul S, Nalinanon S. Compositional and physicochemical characteristics of acid solubilized collagen extracted from the skin of unicorn leatherjacket (Aluterus monoceros). Food Hydrocolloids. 2010;24:588–594. https://doi.org/10.1016/j.foodhyd.2010.03.001
  23. Barzideh Z, Latiff AA, Gan CY, Benjakul S, Karim AA. Isolation and characterisation of collagen from the Ribbon jellyfish (Chrysaora sp.). International Journal of Food Science and Technology. 2014;49(6):1490–1499. https://doi.org/10.1111/ijfs.12464
  24. Li P, Wu G. Roles of dietary glycine, proline, and hydroxyproline in collagen synthesis and animal growth. Amino acids. 2018;50(1):29–38. https://doi.org/10.1007/s00726-017-2490-6
  25. Weber K, Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. Journal of Biological Chemistry. 1969;244(16):4406–4412. https://doi.org/10.1016/S0021-9258(18)94333-4
  26. Felician FF, Yu R-H, Li M-Z, Li C-J, Chen H-Q, et al. The wound healing potential of collagen peptides derived from the jellyfish Rhopilema esculentum. Chinese Journal of Traumatology. 2019;22(1):12–20. https://doi.org/10.1016/j.cjtee.2018.10.004
  27. Kittiphattanabawon P, Benjakul S, Visessanguan W, Shahidi F. Isolation and characterization of collagen from the cartilages of brownbanded bamboo shark (Chiloscyllium punctatum) and blacktip shark (Carcharhinus limbatus). LWT. 2010;43(5):792–800. https://doi.org/10.1016/j.lwt.2010.01.006
  28. Srinivasan S, Durairaj B. Collagen isolation and characterization from Sardinella longiceps. Journal of Advanced Veterinary and Animal Research. 2021;8(4):679–686. https://doi.org/10.5455/javar.2021.h560
  29. Abinaya M, Gayathri M. Biodegradable collagen from Scomberomorus lineolatus skin for wound healing dressings and its application on antibiofilm properties. Journal of cellular biochemistry. 2019;120(9):15572–15584. https://doi.org/10.1002/jcb.28824
  30. Righetti PG. Determination of the isoelectric point of proteins by capillary isoelectric focusing. Journal of chromatography A. 2004;1037(1–2):491–499. https://doi.org/10.1016/j.chroma.2003.11.025
  31. Kantardjieff KA, Rupp B. Protein isoelectric point as a predictor for increased crystallization screening efficiency. Bioinformatics. 2004;20(14):2162–2168. https://doi.org/10.1093/bioinformatics/bth066
  32. Khong NMH, Yusoff FMd, Jamilah B, Basri M, Maznah I, et al. Improved collagen extraction from jellyfish (Acromitus hardenbergi) with increased physical-induced solubilization processes. Food Chemistry. 2018;251:41–50. https://doi.org/10.1016/j.foodchem.2017.12.083
  33. Balikci E, Baran ET, Tahmasebifar A, Yilmaz B. Characterization of collagen from jellyfish Aurelia aurita and investigation of biomaterials potentials. Applied Biochemistry and Biotechnology. 2024;196(6):1–22. https://doi.org/10.1007/s12010-023-04848-5
  34. Vlierberghe SV, Graulus G.-J, Samal KS, Nieuwenhove IV, Dubruel P. Porous hydrogel biomedical foam scaffolds for tissue repair. In Biomedical Foams for Tissue Engineering Applications. 2014;335–390. https://doi.org/10.1533/9780857097033.2.335
  35. Perez-Puyana V, Jiménez-Rosado M, Romero A, Guerrero A. Fabrication and characterization of hydrogels based on gelatinised collagen with potential application in tissue engineering. Polymers. 2020;12(5):1146. https://doi.org/10.3390/polym12051146
  36. Kim M, Jung HY, Jo C. Fundamental study on structural formation, amino acids and nucleotide-related compounds of cultivated meat from 3D-cultured pig muscle stem cells. Food Science and Biotechnology. 2024;34(2):457. https://doi.org/10.1007/s10068-024-01793-9
  37. Ahmad K, Lim JH, Lee EJ, Chun HJ, Ali S, et al Extracellular matrix and the production of cultured meat. Foods. 2021;10(12):3116. https://doi.org/10.3390/foods10123116
  38. Post MJ, Levenberg S, Kaplan DL, Genovese N, Fu J, et al Scientific, sustainability and regulatory challenges of cultured meat. Nature food. 2020;1(7):403–415. https://doi.org/10.1038/s43016-020-0112-z
  39. Gauza-Włodarczyk M, Kubisz L, Włodarczyk D. Amino acid composition in determination of collagen origin and assessment of physical factors effects. International journal of biological macromolecules. 2017;104:987–991. https://doi.org/10.1016/j.ijbiomac.2017.07.013
  40. Moreno HM, Montero MP, Gómez-Guillén MC, Fernández-Martín F, Mørkøre T, et al. Collagen characteristics of farmed Atlantic salmon with firm and soft fillet texture. Food chemistry. 2012;134(2):678–685. https://doi.org/10.1016/j.foodchem.2012.02.160
  41. Cadar E, Pesterau AM, Prasacu I, Ionescu AM, Pascale C, et al. Marine antioxidants from marine collagen and collagen peptides with nutraceuticals applications: A Review. Antioxidants. 2024;13(8):919. https://doi.org/10.3390/antiox13080919
  42. Ryu B, Shin KH, Kim SK. Muscle protein hydrolysates and amino acid composition in fish. Marine Drugs. 2021;19:377–389. https://doi.org/10.3390/md19070377
  43. Emam AN. Collagen and collagen-derived materials: synthesis, structure, classification, fundamental properties and biomedical applications. Discover Applied Sciences. 2025;7(10):1114. https://doi.org/10.1007/s42452-025-07780-x
  44. Zhu M, Li S, Chen L, Cheng C, Yu J, et al. Insights into microstructure, physicochemical characteristics and functional properties of collagen extracted from various livestock skins. Journal of the Science of Food and Agriculture. 2025;105(14):7779–7787. https://doi.org/10.1002/jsfa.70023
  45. Wang J, Wang H, Shi X, Xu L. Research progress on extraction methods, bioactivity, and food industry applications of collagen from livestock and poultry slaughter by-products: A review. Journal of Food Measurement and Characterization. 2026;1–14. https://doi.org/10.1007/s11694-025-03965-5
  46. López-Yoldi M, Riezu-Boj JI, Abete I, Ibero-Baraibar I, Aranaz P, et al. I. Anti-obesity effects of a collagen with low digestibility and high swelling capacity: A human randomized control trial. Nutrients. 2024;16(20):3550. https://doi.org/10.3390/nu16203550
  47. Wang M, Liu Y, Pallarés N, El Marsni Z, Kousoulaki K, et al. Determination of collagen types and mineral contents in fish skin and collagen-containing skin-derived protein hydrolysates before and after in vitro simulated digestion. Food & Function. 2025;16(3):1032–1040. https://doi.org/10.1039/D4FO03137G
  48. Vedakumari SW, Prabakaran L, Pravin YR. Preparation and characterization of marine collagen scaffolds for biomedical applications. Regenerative Engineering and Translational Medicine. 2026;1–8. https://doi.org/10.1007/s40883-025-00554-2
  49. Venkatesan P, Puvvada N, Dash R, Kumar BNP, Sarkar D, et al. The potential of celecoxib-loaded hydroxyapatite-chitosan nanocomposite for the treatment of colon cancer. Biomaterials. 2011;32:3794–806. https://doi.org/10.1016/j.biomaterials.2011.01.027
  50. Hadi J, Brightwell G. Safety of alternative proteins: technological, environmental and regulatory aspects of cultured meat, plant-based meat, insect protein and single-cell protein. Foods. 2021;10:1226. https://doi.org/10.3390/foods10061226
  51. Tahir I, Floreani R. Dual-crosslinked alginate-based hydrogels with tunable mechanical properties for cultured meat. Foods. 2022;11(18):2829. https://doi.org/10.3390/foods11182829
  52. Volkova NA, Yurchenko KA, Degirmendzhi ET, Saenko YuS, Fomochkina II, et al. Bioprinting using extrusion techniques and optimal biomaterials for D-bioprinting of skin components. Crimean Journal of Experimental and Clinical Medicine. 2025;14(4):84–95. (In Russ.)
  53. Norboeva MA, Dzhalilov AT, Sottikulov ES, Norboev AA. Sodium formate production by alkaline oxidation of formaldehyde: Thermal and spectral properties. Chemistry and Biology. 2026;3:33–39. (In Russ.) https://doi.org/10.32743/UniChem.2026.139.1.21557
  54. Makarova EL, Kozhokina OM. Interaction of glucoamylase with collagen by IR spectroscopy. Applied Information Aspects of Medicine. 2025;28(3):85–94. (In Russ.) https://doi.org/10.18499/2070-9277-2025-28-3-85-94
  55. Timchenko PE, Frolov OO, Ryabov NA, Timchenko EV, Volova LT, et al. An algorithm for identifying allogeneic collagen-containing materials for bioink: Optical analysis methods. Optics and Spectroscopy. 2024;132(4):353–357. (In Russ.)
  56. Iqbal B, Muhammad N, Jamal A, Ahmad P, Khan ZUH, et al. An application of ionic liquid for preparation of homogeneous collagen and alginate hydrogels for skin dressing. Journal of Molecular Liquids. 2017;243:720–725. https://doi.org/10.1016/j.molliq.2017.08.101
Download
Contents
Funding
Abstract
Keywords
References