Volume 24, Issue 2 (Iranian South Medical Journal 2021)                   Iran South Med J 2021, 24(2): 88-100 | Back to browse issues page


XML Persian Abstract Print


Download citation:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:

Hajiani E, Osfouri S. Extraction and Purification of Collagen from the Jellyfish Catostylus mosaicus of the Persian Gulf. Iran South Med J 2021; 24 (2) :88-100
URL: http://ismj.bpums.ac.ir/article-1-1437-en.html
1- Department of Chemical Engineering, School of Petroleum, Gas, and Petrochemical Engineering, Persian Gulf University, Bushehr, Iran
2- Department of Chemical Engineering, School of Petroleum, Gas, and Petrochemical Engineering, Persian Gulf University, Bushehr, Iran , osfouri@pgu.ac.ir
Abstract:   (3763 Views)
Background: Collagen is a protein that constitutes a major component of connective tissue and has many applications in the medical and non-medical fields. The increase in the world population and the need for proteins have led to a special focus on seafood. Furthermore, jellyfish is a rich and renewable source of collagen. Therefore, many researchers have shown interest in collagen extraction from jellyfish. This study aims to extract and purify collagen from jellyfish Catostylus mosaicus.
Materials and Methods: Acid-soluble and pepsin-soluble collagens were extracted and purified using a membrane with a MWCO of 100,000 from jellyfish Catostylus mosaicus. Protein content, type, denaturation temperature, and functional groups of the extracted collagens were evaluated using spectrophotometer, electrophoresis, viscometry, and Fourier transform infrared (FTIR) spectroscopy, respectively.
Results: The results showed that pepsin-soluble collagen extracted from the umbrella and arm of the Catostylus mosaicus jellyfish consisted of chains α and dimer β, and the yields of the pepsin-soluble collagens extracted from the jellyfish umbrella and arm were 14.58% and 12.8% of the dry weight. The results also showed that the denaturation temperature of collagen extracted from the jellyfish arm and umbrella were about 27.32  and 28.72 , respectively. The FTIR spectra of pepsin-soluble collagen from the jellyfish umbrella and arm were almost identical to other types of collagens.
Conclusion: The results show that this species of jellyfish can be used as a renewable marine source of collagen instead of other sources of collagens.
Full-Text [PDF 561 kb]   (1765 Downloads)    
Type of Study: Original | Subject: General
Received: 2020/12/2 | Accepted: 2021/02/16 | Published: 2021/05/26

References
1. Balasubramanian P, Prabhakaran MP, Sireesha M, et al. Collagen In Human Tissues: Structure, Function, And Biomedical Implications From A Tissue Engineering Perspective. Adv Polym Sci 2013; 251: 173-206. [DOI:10.1007/12_2012_176]
2. Lee CH, Singla A, Lee Y. Biomedical Applications Of Collagen. Int J Pharm 2001; 221(1-2): 1-22. [DOI:10.1016/S0378-5173(01)00691-3]
3. Giménez B, Turnay J, Lizarbe MA, et al. Use Of Lactic Acid For Extraction Of Fish Skin Gelatin. Food Hydrocolloid 2005; 19(6): 941-50. [DOI:10.1016/j.foodhyd.2004.09.011]
4. Law JX, Liau LL, Saim A, et al. Electrospun Collagen Nanofibers And Their Applications In Skin Tissue Engineering. Tissue Eng Regen Med 2017; 14(6): 699-718. [DOI:10.1007/s13770-017-0075-9] [PMID] [PMCID]
5. Schmidt MM, Dornelles RC, Mello RO, et al. Collagen Extraction Process. Int Food Res J 2016; 23(3): 913-922.
6. Hashim P, Ridzwan MM, Bakar J, et al. Collagen In Food And Beverage Industries. Int Food Res J 2015; 22(1): 1.
7. Rahmani Del Bakhshayesh A, Annabi N, Khalilov R, et al. Recent Advances On Biomedical Applications Of Scaffolds In Wound Healing And Dermal Tissue Engineering. Artif Cells Nanomed Biotechnol 2018; 46(4): 691-705. [DOI:10.1080/21691401.2017.1349778] [PMID]
8. Tangsadthakun C, Kanokpanont S, Sanchavanakit N, et al. Properties Of Collagen/Chitosan Scaffolds For Skin Tissue Engineering. J Met Mater Min 2006; 16(1): 37-44.
9. Zhang D, Wu X, Chen J, et al. The Development Of Collagen Based Composite Scaffolds For Bone Regeneration. Bioact Mater 2018; 3(1): 129-38. [DOI:10.1016/j.bioactmat.2017.08.004] [PMID] [PMCID]
10. Woo T, Lau L, Cheng N, et al. Efficacy Of Oral Collagen In Joint Pain-Osteoarthritis And Rheumatoid Arthritis. J Arthrit 2017; 6(2): 1-4.
11. Fujiwara NH, Kallmes DF, Li ST, et al. Type 1 Collagen As An Endovascular Stent-Graft Material For Small-Diameter Vessels: A Biocompatibility Study. J Vasc Interv Radiol 2005; 16(9): 1229-36. [DOI:10.1097/01.RVI.0000171690.21149.8F] [PMID]
12. Lee A, Hudson AR, Shiwarski DJ, et al. 3D Bioprinting Of Collagen To Rebuild Components Of The Human Heart. Science 2019; 365(6452): 482-7. [DOI:10.1126/science.aav9051] [PMID]
13. Breschi L, Maravic T, Cunha SR, et al. Dentin Bonding Systems: From Dentin Collagen Structure To Bond Preservation And Clinical Applications. Dent Mater 2018; 34(1): 78-96. [DOI:10.1016/j.dental.2017.11.005] [PMID]
14. Al Zahrani R. Extraction And Isolation Of Collagen Type I From Fish Skin [dissertation]. New Zealand: University of Otago, Dunedin, 2011.
15. Noorzai S, Verbeek C, Lay M, et al. Collagen Extraction From Various Waste Bovine Hide Sources. Waste Biomass Valori 2020; 11(11): 5687-98. [DOI:10.1007/s12649-019-00843-2]
16. Gorlov IF, Titov EI, Semenov GV, et al. Collagen From Porcine Skin: A Method Of Extraction And Structural Properties. Int J Food Prop 2018; 21(1): 1031-42. [DOI:10.1080/10942912.2018.1466324]
17. Addad S, Exposito JY, Faye C, et al. Isolation, Characterization And Biological Evaluation Of Jellyfish Collagen For Use In Biomedical Applications. Mar Drugs 2011; 9(6): 967-83. [DOI:10.3390/md9060967] [PMID] [PMCID]
18. Avila Rodriguez MI, Rodriguez Barroso LG, Sánchez ML. Collagen: A Review On Its Sources And Potential Cosmetic Applications. J Cosmet Dermatol 2018; 17(1): 20-6. [DOI:10.1111/jocd.12450] [PMID]
19. Song E, Kim SY, Chun T, et al. Collagen Scaffolds Derived From A Marine Source And Their Biocompatibility. Biomaterials 2006; 27(15): 2951-61. [DOI:10.1016/j.biomaterials.2006.01.015] [PMID]
20. Tibballs J, Yanagihara AA, Turner HC, et al. Immunological And Toxinological Responses To Jellyfish Stings. Inflamm Allergy Drug Targets 2011; 10(5): 438-46. [DOI:10.2174/187152811797200650] [PMID] [PMCID]
21. Taheri N, Mohebbi GH, Vazirizadeh A, et al. The Toxinology Of Jellyfishes; A Systematic Review. Iran South Med J 2013; 16(5): 359-79. (Persian)
22. Poole S, Naidoo R, Edwards J. Creating A Shelf Stable Marinated Jellyfish Product From The Underutilised Species Catostylus Mosaicus. AFFS-Food Technology, Department Of Primary Industries, 2002.
23. Barzideh Z, Latiff AA, Gan CY, et al. Isolation And Characterisation Of Collagen From The Ribbon Jellyfish (Chrysaora Sp.). Int J Food Sci Technol 2014; 49(6): 1490-9. [DOI:10.1111/ijfs.12464]
24. Khong NM, Yusoff FM, Jamilah B, et al. Improved Collagen Extraction From Jellyfish (Acromitus Hardenbergi) With Increased Physical-Induced Solubilization Processes. Food Chem 2018; 251: 41-50. [DOI:10.1016/j.foodchem.2017.12.083] [PMID]
25. Arslan YE, Kantarcıoğlu İ. Salvadora Persica Extract-Laden Jellyfish Collagen Hybrid Constructs For Periodontal Tissue Regeneration. J Turkish Chem Soc Section A: Chem 2019; 6(1): 51-62. [DOI:10.18596/jotcsa.484936]
26. Felician FF, Yu RH, Li MZ, et al. The Wound Healing Potential Of Collagen Peptides Derived From The Jellyfish Rhopilema Esculentum. Chin J Traumatol 2019; 22(1): 12-20. [DOI:10.1016/j.cjtee.2018.10.004] [PMID] [PMCID]
27. Mearns Spragg A, Tilman J, Tams D, et al. The Biological Evaluation Of Jellyfish Collagen As A New Research Tool For The Growth And Culture Of Ipsc Derived Microglia. Front Mar Sci 2020; 7: 689. [DOI:10.3389/fmars.2020.00689]
28. Flaig I, Radenković M, Najman S, et al. In Vivo Analysis Of The Biocompatibility And Immune Response Of Jellyfish Collagen Scaffolds And Its Suitability For Bone Regeneration. Int J Mol Sci 2020; 21(12): 4518. [DOI:10.3390/ijms21124518] [PMID] [PMCID]
29. Pitt KA. Life History And Settlement Preferences Of The Edible Jellyfish Catostylus Mosaicus (Scyphozoa: Rhizostomeae). Mar Biol 2000; 136(2): 269-79. [DOI:10.1007/s002270050685]
30. Coppola D, Oliviero M, Vitale GA, et al. Marine Collagen From Alternative And Sustainable Sources: Extraction, Processing And Applications. Mar Drugs 2020; 18(4): 214. [DOI:10.3390/md18040214] [PMID] [PMCID]
31. Lim YS, Ok YJ, Hwang SY, et al. Marine Collagen As A Promising Biomaterial For Biomedical Applications. Mar Drugs 2019; 17(8): 467. [DOI:10.3390/md17080467] [PMID] [PMCID]
32. Zhang J, Duan R, Huang L, et al. Characterisation Of Acid-Soluble And Pepsin-Solubilised Collagen From Jellyfish (Cyanea Nozakii Kishinouye). Food Chem 2014; 150: 22-6. [DOI:10.1016/j.foodchem.2013.10.116] [PMID]
33. Nagai T, Ogawa T, Nakamura T, et al. Collagen Of Edible Jellyfish Exumbrella. J Sci Food Agric 1999; 79(6): 855-8. https://doi.org/10.1002/(SICI)1097-0010(19990501)79:6<855::AID-JSFA299>3.0.CO;2-N [DOI:10.1002/(SICI)1097-0010(19990501)79:63.0.CO;2-N]
34. Nagai T, Worawattanamateekul W, Suzuki N, et al. Isolation And Characterization Of Collagen From Rhizostomous Jellyfish (Rhopilema Asamushi). Food Chem 2000; 70(2): 205-8. [DOI:10.1016/S0308-8146(00)00081-9]
35. Smith PK, Krohn RI, Hermanson GT, et al. Measurement Of Protein Using Bicinchoninic Acid. Anal Biochem 1985; 150(1): 76-85. [DOI:10.1016/0003-2697(85)90442-7]
36. Walker JM. The Bicinchoninic Acid (BCA) Assay For Protein Quantitation. The Protein Protocols Handbook. United States: Springer, 2009, 11-5. [DOI:10.1007/978-1-59745-198-7_3]
37. Furthmayr H, Timpl R. Characterization Of Collagen Peptides By Sodium Dodecylsulfate-Polyacrylamide Electrophoresis. Anal Biochem 1971; 41(2): 510-6. [DOI:10.1016/0003-2697(71)90173-4]
38. Glassford SE, Byrne B, Kazarian SG. Recent Applications Of ATR FTIR Spectroscopy And Imaging To Proteins. Biochim Biophys Acta 2013; 1834(12): 2849-58. [DOI:10.1016/j.bbapap.2013.07.015] [PMID]
39. Rastian Z, Pütz S, Wang Y, et al. Type I Collagen From Jellyfish Catostylus Mosaicus For Biomaterial Applications. ACS Biomater Sci Eng 2018; 4(6): 2115-25. [DOI:10.1021/acsbiomaterials.7b00979] [PMID]
40. Kittiphattanabawon P, Benjakul S, Visessanguan W, et al. Isolation And Characterization Of Collagen From The Cartilages Of Brownbanded Bamboo Shark (Chiloscyllium Punctatum) And Blacktip Shark (Carcharhinus Limbatus). LWT-Food Sci Technol 2010; 43(5): 792-800. [DOI:10.1016/j.lwt.2010.01.006]
41. Pelton JT, Mclean LR. Spectroscopic Methods For Analysis Of Protein Secondary Structure. Anal Biochem 2000; 277(2): 167-76. [DOI:10.1006/abio.1999.4320] [PMID]
42. Wang L, An X, Xin Z, et al. Isolation And Characterization Of Collagen From The Skin Of Deep‐Sea Redfish (Sebastes Mentella). J Food Sci 2007; 72(8): E450-5. [DOI:10.1111/j.1750-3841.2007.00478.x] [PMID]
43. Ahmad M, Benjakul S, Nalinanon S. Compositional And Physicochemical Characteristics Of Acid Solubilized Collagen Extracted From The Skin Of Unicorn Leatherjacket (Aluterus Monoceros). Food Hydrocolloid 2010; 24(6-7): 588-94. [DOI:10.1016/j.foodhyd.2010.03.001]
44. Cao H, Xu SY. Purification And Characterization Of Type II Collagen From Chick Sternal Cartilage. Food Chem 2008; 108(2): 439-45. [DOI:10.1016/j.foodchem.2007.09.022] [PMID]
45. Pati F, Adhikari B, Dhara S. Isolation And Characterization Of Fish Scale Collagen Of Higher Thermal Stability. Bioresour Technol 2010; 101(10): 3737-42. [DOI:10.1016/j.biortech.2009.12.133] [PMID]
46. Kittiphattanabawon P, Benjakul S, Visessanguan W, et al. Isolation And Characterisation Of Collagen From The Skin Of Brownbanded Bamboo Shark (Chiloscyllium Punctatum). Food Chem 2010; 119(4): 1519-26. [DOI:10.1016/j.foodchem.2009.09.037]
47. Krishnan S, Perumal P. Preparation And Biomedical Characterization Of Jellyfish (Chrysaora Quinquecirrha) Collagen From Southeast Coast Of India. Int J PharmPharm Sci 2013; 5(3): 698-701.

Send email to the article author


Rights and Permissions
Creative Commons License This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.

© 2024 CC BY-NC 4.0 | Iranian South Medical Journal

Designed & Developed by: Yektaweb