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Journal of Polymers and the Environment

, Volume 28, Issue 1, pp 166–178 | Cite as

Fish Scale Collagen Preparation, Characterization and Its Application in Wound Healing

  • Manal ShalabyEmail author
  • Mona Agwa
  • Hesham Saeed
  • Shaimaa M. Khedr
  • Omnia Morsy
  • Maha A. El-Demellawy
Original Paper
  • 124 Downloads

Abstract

A series of fish collagen proteins were prepared for wound healing application. The physicochemical properties such as molecular weight, solubility, thermal stability of the products was studied. Fourier transform infrared spectroscopy (FTIR) was employed to identify the chemical bonds of fish collagen and its resemblance to type 1 collagen. The surface morphology of the prepared collagen was also studied by scanning electron microscopy (SEM). Results obtained showed that Tilapia and Grey mullet collagen consists of identical four subunits including β chains, γ chains and two α chains (α1 and α2). Due to strong fibrillar nature of collagen, it greatly enhances the cell adhesion capacities of the prepared products. Moreover, the antibacterial activity of collagen was investigated. It was found that all the extracted collagen products have inhibitory activity against all of the tested bacteria. Wound healing efficiency of the prepared collagen was also investigated through assessing the rate of wound contraction, histological evaluations demonstrated that collagen treatment resulted in better resolution and closure of the wound. The above analysis suggested that the isolated fish collagen can be a potential candidate for wound healing application.

Keywords

Collagen Wound healing Dressing Collagen gel 

Notes

Acknowledgements

This research has been funded by Academy of Scientifc Research and Technology (ASRT), Grant number 26D/2017.

References

  1. 1.
    Vollmer AN, Rosenfield RG (1983) U.S. Patent No. 4,402,873. U.S. Patent and Trademark Office, Washington, DCGoogle Scholar
  2. 2.
    Berg, RA, Silver FH, Pachence JM (1989) U.S. Patent No. 4,837,285. U.S. Patent and Trademark Office, Washington, DCGoogle Scholar
  3. 3.
    Morimura S, Nagata H, Uemura Y, Fahmi A, Shigematsu T, Kida K (2002) Development of an effective process for utilization of collagen from livestock and fish waste. Process Biochem 37(12):1403–1412CrossRefGoogle Scholar
  4. 4.
    Helcke T (2000) Gelatin, the food technologist’s friend or foe. Int Food Ingred 1:6–8Google Scholar
  5. 5.
    Trevitt CR, Singh PN (2003) Variant Creutzfeldt-Jakob disease: pathology, epidemiology, and public health implications. Am J Clin Nutr 78(3):651S–656SCrossRefGoogle Scholar
  6. 6.
    Gómez-Guillén MC, Giménez B, López-Caballero MA, Montero MP (2011) Functional and bioactive properties of collagen and gelatin from alternative sources: a review. Food Hydrocoll 25(8):1813–1827CrossRefGoogle Scholar
  7. 7.
    Lazovic G, Colic M, Grubor M, Jovanovic M (2005) The application of collagen sheet in open wound healing. Ann Burns Fire Disasters 18(3):151–159PubMedPubMedCentralGoogle Scholar
  8. 8.
    Miller RL, Lee JH, Owens ML (2013) U.S. Patent No. 8,426,457. U.S. Patent and Trademark Office, Washington, DCGoogle Scholar
  9. 9.
    Geistlich P, Schloesser L (2003) U.S. Patent No. 6,576,015. U.S. Patent and Trademark Office, Washington, DCGoogle Scholar
  10. 10.
    Steadman JR, Rodkey WG (2005) Tissue-engineered collagen meniscus implants: 5-to 6-year feasibility study results. Arthroscopy 21(5):515–525CrossRefGoogle Scholar
  11. 11.
    Piez KA, Gross J (1960) The amino acid composition of some fish collagens: the relation between composition and structure. J Biol Chem 235(4):995–998PubMedGoogle Scholar
  12. 12.
    Sood A, Granick MS, Tomaselli NL (2014) Wound dressings and comparative effectiveness data. Adv Wound Care 3(8):511–529CrossRefGoogle Scholar
  13. 13.
    Hoffman AS (2012) Hydrogels for biomedical applications. Adv Drug Deliv Rev 64(1):18–23CrossRefGoogle Scholar
  14. 14.
    Liu J, Chinga-Carrasco G, Cheng F, Xu W, Willför S, Syverud K, Xu C (2016) Hemicellulose-reinforced nanocellulose hydrogels for wound healing application. Cellulose 23(5):3129–3143CrossRefGoogle Scholar
  15. 15.
    Chattopadhyay S, Raines RT (2014) Review collagen-based biomaterials for wound healing. Biopolymers 101(8):821–833CrossRefGoogle Scholar
  16. 16.
    Yamada S, Yamamoto K, Ikeda T, Yanagiguchi K, Hayashi Y (2014) Potency of fish collagen as a scaffold for regenerative medicine. BioMed Res Int 2014:302932CrossRefGoogle Scholar
  17. 17.
    Lee CH, Singla A, Lee Y (2001) Biomedical applications of collagen. Int J Pharm 221(1–2):1–22CrossRefGoogle Scholar
  18. 18.
    Pati F, Datta P, Adhikari B, Dhara S, Ghosh K, Mohapatra PKD (2012) Collagen scaffolds derived from fresh water fish origin and their biocompatibility. J Biomed Mater Res Part A 100(4):1068–1079CrossRefGoogle Scholar
  19. 19.
    Rajan N, Habermehl J, Coté M, Doillon C, Mantovani D (2006) Preparation of ready-to-use, storable and reconstituted type I collagen from rat tail tendon for tissue engineering applications. Nat Protoc 1(6):2753CrossRefGoogle Scholar
  20. 20.
    Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275Google Scholar
  21. 21.
    Sambrook J, Fritsch EF, Maniatis T (1989) Molecular cloning: a laboratory manual, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring HarborGoogle Scholar
  22. 22.
    Laemmli UK, Amos LA, Klug A (1976) Correlation between structural transformation and cleavage of the major head protein of T4 bacteriophage. Cell 7(2):191–203CrossRefGoogle Scholar
  23. 23.
    Baker CN, Stocker SA, Culver DH, Thornsberry C (1991) Comparison of the E Test to agar dilution, broth microdilution, and agar diffusion susceptibility testing techniques by using a special challenge set of bacteria. J Clin Microbiol 29(3):533–538CrossRefGoogle Scholar
  24. 24.
    Magaldi S, Mata-Essayag S, De Capriles CH, Perez C, Colella MT, Olaizola C, Ontiveros Y (2004) Well diffusion for antifungal susceptibility testing. Int J Infect Dis 8(1):39–45CrossRefGoogle Scholar
  25. 25.
    Fayemi OE, Ekennia AC, Katata-Seru L, Ebokaiwe AP, Ijomone OM, Onwudiwe DC, Ebenso EE (2018) Antimicrobial and wound healing properties of polyacrylonitrile-moringa extract nanofibers. ACS Omega 3(5):4791–4797CrossRefGoogle Scholar
  26. 26.
    Johal HS, Garg T, Rath G, Goyal AK (2016) Advanced topical drug delivery system for the management of vaginal candidiasis. Drug Deliv 23(2):550–563CrossRefGoogle Scholar
  27. 27.
    Xie Z, Paras CB, Weng H, Punnakitikashem P, Su LC, Vu K, Tang L, Yang J, Nguyen KT (2013) Dual growth factor releasing multi-functional nanofibers for wound healing. Acta Biomater 9(12):9351–9359CrossRefGoogle Scholar
  28. 28.
    Nagai T, Izumi M, Ishii M (2004) Fish scale collagen. Preparation and partial characterization. Int J Food Sci Technol 39(3):239–244CrossRefGoogle Scholar
  29. 29.
    Cherim M, Sîrbu R (2018) Obtaining of collagen extracts used as biomaterials with applications in the medical field. Eur J Med Nat Sci 2(3):13–18Google Scholar
  30. 30.
    Liao W, Guanghua X, Li Y, Shen XR, Li C (2018) Comparison of characteristics and fibril-forming ability of skin collagen from barramundi (Lates calcarifer) and tilapia (Oreochromis niloticus). Int J Biol Macromol 107:549–559CrossRefGoogle Scholar
  31. 31.
    Rittié L (2017) Type I collagen purification from rat tail tendons fibrosis. Humana Press, New York 2017:287–308Google Scholar
  32. 32.
    Matmaroh K, Benjakul S, Prodpran T, Encarnacion AB, Kishimura H (2011) Characteristics of acid soluble collagen and pepsin soluble collagen from scale of spotted golden goatfish (Parupeneus heptacanthus). Food Chem 129(3):1179–1186CrossRefGoogle Scholar
  33. 33.
    Tamilmozhi S, Veeruraj A, Arumugam M (2013) Isolation and characterization of acid and pepsin-solubilized collagen from the skin of sailfish (Istiophorus platypterus). Food Res Int 54(2):1499–1505CrossRefGoogle Scholar
  34. 34.
    Okazaki E, Osako K (2014) Isolation and characterization of acid-soluble collagen from the scales of marine fishes from Japan and Vietnam. Food Chem 149:264–270CrossRefGoogle Scholar
  35. 35.
    Sinthusamran S, Benjakul S, Kishimura H (2013) Comparative study on molecular characteristics of acid soluble collagens from skin and swim bladder of seabass (Lates calcarifer). Food Chem 138(4):2435–2441CrossRefGoogle Scholar
  36. 36.
    Tziveleka LA, Ioannou E, Tsiourvas D, Berillis P, Foufa E, Roussis V (2017) Collagen from the marine sponges Axinella cannabina and Suberites carnosus: isolation and morphological, biochemical, and biophysical characterization. Marine Drugs 15(6):152–168CrossRefGoogle Scholar
  37. 37.
    Kaewdang O, Benjakul S, Kaewmanee T, Kishimura H (2014) Characteristics of collagens from the swim bladders of yellowfin tuna (Thunnus albacares). Food Chem 15(155):264–270CrossRefGoogle Scholar
  38. 38.
    Singh P, Benjakul S, Maqsood S, Kishimura H (2011) Isolation and characterisation of collagen extracted from the skin of striped catfish (Pangasianodon hypophthalmus). Food Chem 124(1):97–105CrossRefGoogle Scholar
  39. 39.
    Zhang J, Duan R, Huang L, Song Y, Regenstein JM (2014) Characterisation of acid-soluble and pepsin-solubilised collagen from jellyfish (Cyanea nozakii Kishinouye). Food Chem 1(150):22–26CrossRefGoogle Scholar
  40. 40.
    Doyle BB, Bendit EG, Blout ER (1975) Infrared spectroscopy of collagen and collagen-like polypeptides. Biopolymers 14(5):937–957CrossRefGoogle Scholar
  41. 41.
    Krimm S, Abe Y (1972) Intermolecular interaction effects in the amide I vibrations of β polypeptides. Proc Natl Acad Sci USA 69(10):2788–2792CrossRefGoogle Scholar
  42. 42.
    Muyonga JH, Cole CGB, Duodu KG (2004) Fourier transform infrared (FTIR) spectroscopic study of acid soluble collagen and gelatin from skins and bones of young and adult Nile perch (Lates niloticus). Food Chem 86(3):325–332CrossRefGoogle Scholar
  43. 43.
    Bryan MA, Brauner JW, Anderle G, Flach CR, Brodsky B, Mendelsohn R (2007) FTIR studies of collagen model peptides: complementary experimental and simulation approaches to conformation and unfolding. J Am Chem Soc 129(25):7877–7884CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  • Manal Shalaby
    • 1
    Email author
  • Mona Agwa
    • 2
  • Hesham Saeed
    • 3
  • Shaimaa M. Khedr
    • 4
  • Omnia Morsy
    • 1
  • Maha A. El-Demellawy
    • 1
  1. 1.Department of Medical Biotechnology, Institute of Genetic EngineeringCity of Scientific Research and Technology ApplicationsNew Borg El Arab, AlexandriaEgypt
  2. 2.Department of Natural and Microbial ProductsNational Research CentreCairoEgypt
  3. 3.Department of Biotechnology, Institute of Graduate Studies and ResearchAlexandria UniversityAlexandriaEgypt
  4. 4.Pharmaceutical & Fermentation Industries Development Center (PFIDC)City of Scientific Research and Technology ApplicationsNew Borg El Arab, AlexandriaEgypt

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