Fisheries and Aquatic Sciences

The Korean Society of Fisheries and Aquatic Science (한국수산과학회)
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Extraction and characterization of pepsin-soluble collagen from different mantis shrimp species

  • Received : 2021.10.05
  • Accepted : 2021.10.26
  • Published : 2021.12.31
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Abstract

The objective of this study was to investigate the yield and characteristics of collagen protein extracted from the muscle of four different species of mantis shrimp: Miyakella nepa, Harpiosquilla harpax, Erugosquilla woodmasoni, and Odontodactylus cultrifer. Mantis shrimp muscle was extracted by using a pepsin-solubilization technique, with 0.5 M acetic acid and 5% pepsin enzyme. The highest collagen yield was from M. nepa muscle (0.478 ± 0.06%), which was significantly greater (p < 0.05) than that from H. harpax, O. cultrifer, and E. woodmasoni (0.313 ± 0.03%, 0.123 ± 0.02%, and 0.015 ± 0.00%, respectively). The freeze-dried collagen appeared as thin fibers, and formed an opaque film. The pepsin-soluble collagen (PSC) from four mantis shrimp species was analyzed by gel electrophoresis. The results showed that all species of mantis shrimp contained type I collagen, consisting of β, α1, and α2 subunits with average molecular weights of 250, 145, and 118 kDa, respectively. The study of the solubility of collagen showed that, for NaCl, collagen had the highest relative solubility in 2% NaCl (80.20 ± 4.95%). In contrast, the solubility decreased at higher NaCl concentrations. However, in terms of pH, collagen had the highest relative solubility at pH 3 (91.32 ± 5.14%), and its solubility decreased at higher pH. FT-IR spectroscopy was used to compare the collagen with a model compound. Five wavenumbers in the spectrum for model collagen were identified: Amide A (3,406-3,421 cm-1), amide B (2,916-2,940 cm-1), amide I (1,639-1,640 cm-1), amide II (1,539-1,570 cm-1), and amide III (1,234-1,250 cm-1).

Keywords

Acknowledgement

Special thanks to Faculty of Gems and Faculty of Marine Technology, Burapha University for providing facilities and research equipment.

References

  1. Ahmed R, Haq M, Chun BS. Characterization of marine derived collagen extracted from the by-products of bigeye tuna (Thunnus obesus). Int J Biol Macromol. 2019;135:668-76. https://doi.org/10.1016/j.ijbiomac.2019.05.213
  2. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976;72:248-54. https://doi.org/10.1006/abio.1976.9999
  3. Cheng X, Shao Z, Li C, Yu L, Raja MA, Liu C. Isolation, characterization and evaluation of collagen from jellyfish Rhopilema esculentum kishinouye for use in hemostatic applications. PLOS ONE. 2017;12:e0169731. https://doi.org/10.1371/journal.pone.0169731
  4. Ciarlo AS, Paredi ME, Fraga AN. Isolation of soluble collagen from hake skin (Merluccius hubbsi). J Aquat Food Prod Technol. 1997;6:65-77. https://doi.org/10.1300/J030v06n01_06
  5. Duan R, Zhang J, Du X, Yao X, Konno K. Properties of collagen from skin, scale and bone of carp (Cyprinus carpio). Food Chem. 2009;112:702-6. https://doi.org/10.1016/j.foodchem.2008.06.020
  6. Foegeding EA, Lanier TC, Hultin HO. Collagen. In: Fennema OR, editor. Food chemistry. 3rd ed. New York, NY: Marcel Dekker; 1996. p. 902-6.
  7. Jafari H, Lista A, Siekapen MM, Ghaffari-Bohlouli P, Nie L, Alimoradi H, et al. Fish collagen: extraction, characterization, and applications for biomaterials engineering. Polymers. 2020;12:1-37.
  8. Jongjareonrak A, Benjakul S, Visessanguan W, Nagai T, Tanaka M. Isolation and characterisation of acid and pepsin-solubilised collagens from the skin of Brownstripe red snapper (Lutjanus vitta). Food Chem. 2005;93:475-84. https://doi.org/10.1016/j.foodchem.2004.10.026
  9. Jose HMPM, Murugesan P, Arumugam M, Kumar KM. Isolation and characterization of acid and pepsin-solubilised collagen from the muscle of mantis shrimp (Oratosquilla nepa). Int J Pharm Pharm Sci. 2014;6:654-7.
  10. Khong NMH, Yusoff FM, Jamilah B, Basri M, Maznah I, Chan KW, et al. Improved collagen extraction from jellyfish (Acromitus hardenbergi) with increased physical-induced solubilization processes. Food Chem. 2018;251:41-50. https://doi.org/10.1016/j.foodchem.2017.12.083
  11. Kittiphattanabawon P, Benjakul S, Visessanguan W, Nagai T, Tanaka M. Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus). Food Chem. 2005;89:363-72. https://doi.org/10.1016/j.foodchem.2004.02.042
  12. Kutako M, Tocharoen T, Sonthi M, Hiransuchalert R, Watanachote J. Yield and protein pattern of collagen extracted from Greenback mullet (Liza subviridis) scale by different pepsin concentrations. Khon Kaen Agric J. 2016;43:562-7.
  13. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227:680-5. https://doi.org/10.1038/227680a0
  14. Lin S, Xue YP, San E, Keong TC, Chen L, Zheng YG. Extraction and characterization of pepsin soluble collagen from the body wall of sea cucumber Acaudina leucoprocta. J Aquat Food Prod Technol. 2017;26:502-15. https://doi.org/10.1080/10498850.2016.1222560
  15. Liu Z, Oliveira ACM, Su YC. Purification and characterization of pepsin-solubilized collagen from skin and connective tissue of giant red sea cucumber (Parastichopus californicus). J Agric Food Chem. 2010;58:1270-4. https://doi.org/10.1021/jf9032415
  16. Meyer M. Processing of collagen based biomaterials and the resulting materials properties. Biomed Eng Online. 2019;18:1-74. https://doi.org/10.1186/s12938-019-0647-0
  17. Mizuta S, Yoshinaka R, Sato M, Sakaguchi M. Characterization of collagen in the muscle of several crustacean species in association with raw meat texture. Fish Sci. 1994;60:323-8. https://doi.org/10.2331/fishsci.60.323
  18. Montero P, Borderias J, Turnay J, Leyzarbe MA. Characterization of hake (Merluccius merluccius L.) and trout (Salmo irideus Gibb) collagen. J Agric Food Chem. 1990;38:604-9. https://doi.org/10.1021/jf00093a004
  19. Morimura S, Nagata H, Uemura Y, Fahmi A, Shigematsu T, Kida K. Development of an effective process for utilization of collagen from livestock and fish waste. Process Biochem. 2002;37:1403-12. https://doi.org/10.1016/S0032-9592(02)00024-9
  20. Nagai T, Suzuki N. Isolation of collagen from fish waste material - skin, bone and fins. Food Chem. 2000;68:277-81. https://doi.org/10.1016/S0308-8146(99)00188-0
  21. Pati F, Adhikari B, Dhara S. Isolation and characterization of fish scale collagen of higher thermal stability. Bioresour Technol. 2010;101:3737-42. https://doi.org/10.1016/j.biortech.2009.12.133
  22. Plepis AMDG, Goissis G, Das-Gupta DK. Dielectric and pyroelectric characterization of anionic and native collagen. Polym Eng Sci. 1996;36:2932-8. https://doi.org/10.1002/pen.10694
  23. Saallah S, Roslan J, Julius FS, Saallah S, Mohamad Razali UH, Pindi W, et al. Comparative study of the yield and physicochemical properties of collagen from sea cucumber (Holothuria scabra), obtained through dialysis and the ultrafiltration membrane. Molecules. 2021;26:2564. https://doi.org/10.3390/molecules26092564
  24. Sadowska M, Kolodziejska L, Niecikowska C. Isolation of collagen from the skins of Baltic cod (Gadus morhua). Food Chem. 2003;81:257-62. https://doi.org/10.1016/S0308-8146(02)00420-X
  25. Shoulders MD, Raines RT. Collagen structure and stability. Annu Rev Biochem. 2009;78:929-58. https://doi.org/10.1146/annurev.biochem.77.032207.120833
  26. Tabarestani HS, Maghsoudlou Y, Motamedzadegan A, Sadeghi Mahoonak AR, Rostamzad H. Study on some properties of acid-soluble collagens isolated from fish skin and bones of rainbow trout (Onchorhynchus mykiss). Int Food Res J. 2012;19:251-7.
  27. Tziveleka LA, Ioannou E, Tsiourvas D, Berillis P, Foufa E, Roussis V. Collagen from the marine sponges Axinella cannabina and Suberites carnosus: isolation and morphological, biochemical, and biophysical characterization. Mar Drugs. 2017;15:152. https://doi.org/10.3390/md15060152
  28. Veeruraj A, Arumugam M, Ajithkumar T, Balasubramanian T. Isolation and characterization of collagen from the outer skin of squid (Doryteuthis singhalensis). Food Hydrocoll. 2015;43:708-16. https://doi.org/10.1016/j.foodhyd.2014.07.025
  29. Vojdani F. Solubility. In: Methods of testing protein functionality. London, UK: Blackie Academic & Professional; 1996. p. 11-60.