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Application of ultrasonic treatment to extraction of collagen from the skins of sea bass Lateolabrax japonicus

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Abstract

This study investigates an efficient method to extract collagen from the skins of sea bass. The ultrasonic treatment (20 kHz with amplitude of 20–80 %) was applied to fish skin for 24 h after the addition of 0.01, 0.05, and 0.1 M acetic acid (1:200 sample/acetic acid, w/v). As a result, the rate (Ki) of the collagen yield increased depending on the amount of acid added, the duration of ultrasonic treatment and the amplitude of the ultrasonic waves. The subunit compositions of the extracted components were analyzed by SDS-PAGE, and the main components were determined as collagen, including the α1 (α3), α2, β, and γ chains. And in addition to collagen, some unknown components were also observed after a longer period of ultrasonic treatment. Therefore, we had to optimize the efficient extraction conditions for pure collagen while minimizing the creation of unknown components. The most effective extraction condition for collagen by ultrasonic treatment was 80 % amplitude with 0.1 M acetic acid for 3 h of treatment. It was found that the component extracted by the ultrasonic treatment was indeed collagen, since there were no changes in the main components of collagen after pepsin treatment.

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References

  1. Bracho GE, Haard NF (1990) Determination of collagen crosslinks in rockfish skeletal muscle. J Food Biochem 14:435–451

    Article  Google Scholar 

  2. Sikorski ZE, Scott DN, Buisson DH (1984) The role of collagen in the quality and processing of fish. Crit Rev Food Sci Nutr 20:301–343

    Article  PubMed  CAS  Google Scholar 

  3. Leuenberger BH (1991) Investigation of viscosity and gelatin properties of different mammalian and fish gelatins. Food Hydrocoll 41:353–361

    Article  Google Scholar 

  4. Kimura S (1992) Wide distribution of skin Type I collagen α3-chain in bony fish. Comp Biochem Physiol B 102:255–260

    PubMed  CAS  Google Scholar 

  5. Kimura S, Miyauchi Y, Uchida N (1991) Scale and bone Type I collagens of carp (Cyprinus carpio). Comp Biochem Physiol B 99:473–476

    Article  PubMed  CAS  Google Scholar 

  6. Kimura S, Ohno Y (1987) Fish Type I collagen: tissue specific existence of two molecular forms (α1)2, α2 and α1α2α3, in Alaska pollock. Comp Biochem Physiol B 88:409–413

    Google Scholar 

  7. Ciarlo AS, Paredi ME, Fraga AN (1997) Isolation of soluble collagen from hake skin (Merluccius hubbsi). J Aquac Food product Tech 6:65–77

    Article  CAS  Google Scholar 

  8. HO H, Lin LH, Sheu MT (1997) Characterization of collagen isolation and application of collagen gel as a drug carrier. J Controlled Release 44:103–112

    Article  CAS  Google Scholar 

  9. John FC, Paul DF, Karl HK (1993) Collagen fabrics as biomaterials. Biotech Bioeng 43:781–791

    Google Scholar 

  10. Takeshi N, Nobutaka S (2000) Isolation of collagen from fish waste material: skin, bone and fins. Food Chem 68:277–281

    Article  Google Scholar 

  11. Kim HK, Kim YH, Kim YJ, Park HJ, Lee NH (2012) Effects of ultrasonic treatment on collagen extraction from skins of the sea bass Lateolabrax japonicas. Fish Sci 78:485–490

    Article  Google Scholar 

  12. Kruus P, O’Neill M, Robertson D (1990) Ultrasonic initiation of polymerization. Ultrasonics 28:304–309

    Article  CAS  Google Scholar 

  13. AOAC Association of Official Analytical Chemists (1999) In: K. Helrich (ed) Official methods analysis, 14th edn Washington, DC

  14. Gornall AG, Bardawill CJ, David MM (1949) Determination of serum proteins by means of the biuret reaction. J Biol Chem 177:751–766

    PubMed  CAS  Google Scholar 

  15. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685

    Article  PubMed  CAS  Google Scholar 

  16. Floros JD, Liang H (1994) Acoustically assisted diffusion through membranes and biomaterials. Food Technol 48:79–84

    Google Scholar 

  17. Crum L (1995) Comments on the evolving field of sonochemistry by a cavitation physicist. Ultrason Sonochem 2:S147–S152

    Article  CAS  Google Scholar 

  18. Ana CS, Mar V (2010) Effect of ultrasound on the technological properties and bioactivity of food: a review. Trends Food Sci Technol 21:323–331

    Article  Google Scholar 

  19. Lawrence SB, Mitchell RZ, Edward BF, Kenneth SS (1996) Cavitation thermometry using molecular and continuum sololuminescence. J Phys Chem 100:6612–6619

    Article  Google Scholar 

  20. Lawrence AC (1995) Comments on the evolving field of sonochemistry by a cavitation physicist. Ultrasonic sonochem 2:147–152

    Article  Google Scholar 

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Acknowledgments

This study was supported by the research fund from Korea Food Research Institute, Korea.

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Correspondence to Nam Hyouck Lee.

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Kim, H.K., Kim, Y.H., Park, H.J. et al. Application of ultrasonic treatment to extraction of collagen from the skins of sea bass Lateolabrax japonicus . Fish Sci 79, 849–856 (2013). https://doi.org/10.1007/s12562-013-0648-z

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  • DOI: https://doi.org/10.1007/s12562-013-0648-z

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