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Isolation and properties of acid- and pepsin-soluble collagen from the skin of blacktip shark (Carcharhinus limbatus)

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Abstract

Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from the skin of blacktip shark (Carcharhinus limbatus) were isolated and characterized. The yield of ASC (20.01%) was much higher than that of PSC isolated from the residue of ASC extraction (0.86%). Both collagens had protein as their major constituent with the trace amounts of ash and fat. Based on protein patterns and TOYOPEARL® CM-650M column chromatography, both collagens contained α- and β-chains as their main components and were characterized as type I collagen with the cross-link of α2-chain. Similar peptide maps of both collagens, digested by either V8 protease or lysyl endopeptidase, were observed but they were totally different from those of type I collagen from calf skin hydrolyzed by the same enzyme. Thermal transition temperature (T max) of ASC and PSC were 34.23 and 34.37 °C, respectively. Fourier-transform infrared spectra suggested that both collagens were in triple-helical structure. From zeta potential analysis, isoelectric points (pI) of ASC and PSC were estimated to be 6.78 and 7.02, respectively. Thus, blacktip shark skin may serve as an alternative source of collagen and acid solubilization process could be implemented with ease and high yield.

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References

  1. Balian G, Bowes JH (1977) In: Ward AG, Courts A (eds) The science and technology of gelatin, Academic Press, London

  2. Sadowska M, Kolodziejska I, Niecikowska C (2003) Food Chem 81:257–262

    Article  CAS  Google Scholar 

  3. Regenstein JM, Zhou P (2007) In: Shahidi F (ed) Maximising the value of marine by-products, 1st edn. Woodhead Publishing Limited, Cambridge

  4. Musick JA (2005) In: Musick JA, Bonfil R (eds) Management techniques for elasmobranch fisheries. FAO fisheries technical paper no. 474, FAO, Rome

  5. Bae I, Osatomi K, Yoshida A, Osako K, Yamaguchi A, Hara K (2008) Food Chem 108:49–54

    Article  CAS  Google Scholar 

  6. Hwang JH, Mizuta S, Yokoyama Y, Yoshinaka R (2007) Food Chem 100:921–925

    Article  CAS  Google Scholar 

  7. Nomura Y (2004) Dev Food Sci 42:147–158

    Article  CAS  Google Scholar 

  8. AOAC (2000) Official methods of analysis. Association of Official Analytical Chemists Inc, Arlington

    Google Scholar 

  9. Nalinanon S, Benjakul S, Visessanguan W, Kishimura H (2008) J Food Sci 73:C413–C419

    Article  CAS  Google Scholar 

  10. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) J Biol Chem 193:265–275

    CAS  Google Scholar 

  11. Kittiphattanabawon P, Benjakul S, Visessanguan W, Nagai T, Tanaka M (2005) Food Chem 89:363–372

    Article  CAS  Google Scholar 

  12. Nalinanon S, Benjakul S, Visessanguan W, Kishimura H (2007) Food Chem 104:593–601

    Article  CAS  Google Scholar 

  13. Laemmli UK (1970) Nature 227:680–685

    Article  CAS  Google Scholar 

  14. Nagai T, Suzuki N, Nagashima T (2008) Food Chem 111:296–301

    Article  CAS  Google Scholar 

  15. Jongjareonrak A, Benjakul S, Visessanguan W, Nagai T, Tanaka M (2005) Food Chem 93:475–484

    Article  CAS  Google Scholar 

  16. Duan R, Zhang J, Du X, Yao X, Konno K (2009) Food Chem 112:702–706

    Article  CAS  Google Scholar 

  17. Foegeding EA, Lanier TC, Hultin HO (1996) In: Fennema OR (ed) Food chemistry. Marcel Dekker, New York

  18. Muyonga JH, Cole CGB, Duodu KG (2004) Food Chem 85:81–89

    Article  CAS  Google Scholar 

  19. Kimura S, Kamimura T, Takema Y, Kubota M (1981) BBA Protein Struct 669:251–257

    CAS  Google Scholar 

  20. Jekel PA, Weijer WJ, Beintema JJ (1983) Anal Biochem 134:347–354

    Article  CAS  Google Scholar 

  21. Vercaigne-Marko D, Kosciarz E, Nedjar-Arroume N, Guillochon D (2000) Biotechnol Appl Biochem 31:127–134

    Article  CAS  Google Scholar 

  22. Wang L, An X, Xin Z, Zhao L, Hu Q (2007) J Food Sci 72:E450–E455

    Article  CAS  Google Scholar 

  23. Damodaran S (1996) In: Fennema OR (ed) Food chemistry, Marcel Dekker, New York

  24. Muyonga JH, Cole CGB, Duodu KG (2004) Food Chem 86:325–332

    Article  CAS  Google Scholar 

  25. Payne KJ, Veis A (1988) Biopolymers 27:1749–1760

    Article  CAS  Google Scholar 

  26. Surewicz WK, Mantsh HH (1988) Biochim Biophys Acta 952:115–130

    CAS  Google Scholar 

  27. Plepis AMDG, Goissis G, Das-Gupta DK (1996) Polym Eng Sci 36:2932–2938

    Article  Google Scholar 

  28. Doyle BB, Blout ER, Bendit EG (1975) Biopolymers 14:937–957

    Article  CAS  Google Scholar 

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Acknowledgments

This research was supported by grant from under the program Strategic Scholarships for Frontier Research Network for the Joint PhD Program Thai Doctoral degree from the Office of the Higher Education Commission, Thailand. Authors would like to thank the Prince of Songkla University for the financial support, Professor Dr. Hideki Kishimura of laboratory of Marine Products and Food Science, Research Faculty of Fisheries Sciences, Hokkaido University, Japan, for his assistance in amino acid analysis and Mr. Veera Prateeptintong, a managing director of Blue Ocean Food Products, Co., Ltd., Samutsakhon Province, Thailand, for kindly providing blacktip shark skin.

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Correspondence to Soottawat Benjakul.

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Kittiphattanabawon, P., Benjakul, S., Visessanguan, W. et al. Isolation and properties of acid- and pepsin-soluble collagen from the skin of blacktip shark (Carcharhinus limbatus). Eur Food Res Technol 230, 475–483 (2010). https://doi.org/10.1007/s00217-009-1191-0

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  • DOI: https://doi.org/10.1007/s00217-009-1191-0

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