Fisheries and Aquatic Sciences

The Korean Society of Fisheries and Aquatic Science (한국수산과학회)
권호 표지
DOI QR코드

DOI QR Code

Isolation and Characterization of Collagen from Skin of Bullfrog, Rana catesbeiana Shaw

  • Qian, Zhong-Ji (Department of Chemistry, Pukyong National University) ;
  • Jung, Won-Kyo (Department of NOAA Sea Grant College Program, Louisiana State University) ;
  • Ngo, Nghiep Dai (Department of Chemistry, Pukyong National University) ;
  • Lee, Sang-Hoon (Department of Chemistry, Pukyong National University) ;
  • Kim, Se-Kwon (Department of Chemistry, Pukyong National University)
  • Published : 2007.06.30
Download PDF
⟨ Previous Next ⟩

Abstract

In order to utilize skin of bullfrog (Rana catesbeiana Shaw) as an alternative source of collagen, we investigated and compared biochemical and physical properties of collagens isolated from bullfrog skin. Two kinds of collagen (BSASC; bullfrog skin acid-soluble collagen and BSPSC; bullfrog skin pepsin-solubilized collagen) were isolated by subsequent treatments with acetic acid and pepsin. The amounts of skin collagen isolated in the subsequent treatments were 7.3% BSASC and 18.2% BSPSC on the basis of lyophilized bullfrog skin weight, respectively. According to the electrophoretic pattern and CM-cellulose column chromatogram, the BSASC has the chain composition of ${\alpha}1{\alpha}2{\alpha}3$ heterotrimer, and the BSPSC consists of two ${\alpha}$ chains of ${\alpha}1{\alpha}2$. In addition, the denaturation temperatures of all collagens tested were ranged from $30^{\circ}C\;to\;38^{\circ}C$. This study suggests that there is a possibility to use bullfrog skin collagen as an alternative source of collagen for industrial purposes, and subsequently it may increase the economical value of the bullfrog.

Keywords

References

  1. Bailey, A.J and N.D. Light. 1989. Connective Tissue in Meat and Meat Products. Elsevier Applied Science, London
  2. Cavallaro, J.F., P.O. Kemp and K.H. Kraus. 1994. Collagen fabrics as biomaterials. Biotechnol. Bioeng., 43, 781-791 https://doi.org/10.1002/bit.260430813
  3. Foegeding, E.A., T.C, Lanier and H.O. Hultin. 1996. Collagen. In: Fennema, O.R.(Ed.), Food Chemistry. Marcel Dekker Inc, New York, pp. 902-906
  4. Hclcke, I. 2000. Gelatin, the food technologist's friend or foe? Int. Food Ingredients, 1,6-8
  5. Hood, L.L. 1987. Collagen in sausage casings. In A. M. Pearson, I. R. Dutson. and A. J. Bailey (Eds.), Advan-ces in Meat Research, vol. 4: Collagen as Food. Nost-rand Reinhold, New York, pp. 109-129
  6. Keiji, F., M. Miho, H, Takami and S. Akihiko. 1998. Protein release from collagen matrices. Adv. Drug Deliv. Rev., 31, 247-266 https://doi.org/10.1016/S0169-409X(97)00119-1
  7. Kim, S.K., O.J. Kang and D.C. Kwak. 1993. Physicochemical characteristics of filefish and cod skin collagen. J. Kor. Agric. Chem, Soc., 36, 163-171
  8. Kimura, S. and Y. Ohno. 1987. Fish type I collagen: tissue-specific existence of two molecular forms, ($\alpha$1)2$\alpha$2 and $\alpha$1$\alpha$ 2$\alpha$3, in alaska Pollack. Comp. Biochem. Physiol., 88B, 409-413
  9. Kimura, S., Y. Ohno, Y. Miyauchi and N. Uchida. 1987. Fish skin type I collagen: wide distribution of an $\alpha$3 subunit in teleosts. Comp. Biochem, Physiol., 88B, 27-34
  10. Kimura, S., Y. Takerna and M. Kubota. 1981. Octopus skin collagen. Isolation and characterization of collagen comprising two distinct alpha chains. J. Biol. Chem., 256, 13230-13234
  11. Kimura, S., X.P. Zhu, R. Matsui, M. Shijoh and S. Takamizawa. 1988. Characterization of fish musele Type I collagen. J. Food Sci., 53,1315-1318 https://doi.org/10.1111/j.1365-2621.1988.tb09266.x
  12. Kimura, S. 1985. The interstitial collagens of fish. In A. Bairati and R. Garrone (Eds.), Biology of Invertebrate and Lower Vertebrate Collagens. Plenum Press, New York, pp. 399-408
  13. Laernrnli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London), 227, 680-685 https://doi.org/10.1038/227680a0
  14. Marie-Madeleine, G.G., B. Laurence, C. Christine, D. Patrick and H. Daniel. 2000. Structural aspects of fish skin collagen which forms ordered arrays via liquid crystalline states. Biornaterials, 21, 899-906
  15. Mizuts, S., J. Hwang and R. Yoshinaka. 2002. Molecular species of collagen from wing muscle of state (Raja kenojei). Food Chem., 76, 53-58 https://doi.org/10.1016/S0308-8146(01)00249-7
  16. Nagai, T., Y. Araki and N. Suzuki. 2002. Collagen of the skin of ocellate puffer fish (Takifugu rubripes). Food Chem., 78, 173-177 https://doi.org/10.1016/S0308-8146(01)00396-X
  17. Nagai, T., M. Izumi and M. Ishii. 2004. Fish scale collagen. Preparation and partial characterization. Int. J. Food Sci. Technol., 39, 239-244 https://doi.org/10.1111/j.1365-2621.2004.00777.x
  18. Nagai, T., T. Ogawa, T. Nakamura, T. Ito, H. Nakagawa, K. Fujikii, M. Nakao and T. Yano. 1999. Collagen of edible jellyfish exumbrella. J. Sci. Food Agric., 9, 855-858
  19. Nagai, T. and N. Suzuki. 2002. Preparation and partial characterization of collagen from paper nautilus (Argonauta argo, Linnaeus) outer skin. Food Chem., 76,149-153 https://doi.org/10.1016/S0308-8146(01)00255-2
  20. Nagai, T., W. Worawattanamateekul, N. Suzuki, T. Nakamura, T. Ito, K. Fujiki, M. Nakao and T. Yano. 2000. Isolation and characterization of collagen from rhizostomous jellyfish (Rhopilema asamushi). Food Chem., 70, 205-208 https://doi.org/10.1016/S0308-8146(00)00081-9
  21. Nagai, T., E. Ymashita, K. Taniguchi, N, Kanamori and N. Suzuki. 2001. Isolation and characterization of collagen from the outer skin waste material of cuttlefish (Sepia Lycidas). Food Chem., 72, 425-429 https://doi.org/10.1016/S0308-8146(00)00249-1
  22. Piez, K.A. 1965. Characterization of a collagen from codfish skin containing three chromatographically different a chains. Biochem., 4, 2590-2596 https://doi.org/10.1021/bi00888a007
  23. Pitchumani, S., S. Lonchin and C. Gowri. 2000. Molecular species of collagen in the intramuscular connective tissues of the marine crab, Scylla serrata. Comp. Biochem. Physiol. Part B. 125, 555-562 https://doi.org/10.1016/S0305-0491(00)00167-X
  24. Senaratne, L.S., P.J. Park and S.K. Kim. 2006. Isolation and characterization of collagen from brown backed toadfish (Lagocephalus gloveri) skim. Bioresource. Technol., 97,191-197 https://doi.org/10.1016/j.biortech.2005.02.024
  25. Ramachandran, G.N. 1988. Stereochemistry of collagen. Int. J. Peptide Protein Res., 31, 1-16 https://doi.org/10.1111/j.1399-3011.1988.tb00001.x
  26. Shanmugasundaram, N., P. Ravichandran, P. Neelakanta Reddy, R. Nalini, P. Subrata and K. Panduranga Rao. 2001. Collagen chistan polymeric scaffolds for the in vitro culture of human epidermoid carcinoma cells. Biomaterials, 22, 1943-1951 https://doi.org/10.1016/S0142-9612(00)00220-9
  27. Slade, L. and H. Levine. 1987. Polymer-chemical properties of gelatin in foods. In A. M. Pearson, T. R. Dutson, and A. J. Bailey (Eds.), Advances in Meat Research, vol. 4, Collagen as Food. Nostrand Reinhold, New York, pp. 251-266
  28. Stainsby, G. 1987. Gelatin gels. In A. M. Pearson, T. R. Dutson and A. J. Bailey (Eds.), Advances in Meat Research, vol. 4, Collagen as Food. Nostrand Reinhold, New York, pp. 209-222
  29. Willoughby, C.E., M. Batterbury and S.B. Kaye, S.B. 2002. Collagen corneal shields. Surv. Ophthalmol., 47, 174-182 https://doi.org/10.1016/S0039-6257(01)00304-6
  30. Wolfgang, F. 1998. Collagen-biomaterial for drug delivery. Eur. J. Pharm. Biopharm., 45, 113-136 https://doi.org/10.1016/S0939-6411(98)00017-4
  31. Yamashita, M.S., S. Arai, S. Kokubo, K. Aso, and M. Fujimaki. 1975. Synthesis and characterization of a glutamic acid enriched plastein with greater solubility. J. Agric. Food. Chem., 23, 27-30 https://doi.org/10.1021/jf60197a027

Cited by

  1. Prospective of the Cosmeceuticals Derived from Marine Organisms vol.13, pp.5, 2007, https://doi.org/10.1007/s12257-008-0113-5