Fisheries and Aquatic Sciences

The Korean Society of Fisheries and Aquatic Science (한국수산과학회)
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Physicochemical Properties of Gelatin from Jellyfish Rhopilema hispidum

  • Cho, Suengmok (Korea Food Research Institute) ;
  • Ahn, Ju-Ryun (Department of Food Science and Technology/Institute of Food Science, Pukyong National University) ;
  • Koo, Ja-Sung (Department of Food Science and Technology/Institute of Food Science, Pukyong National University) ;
  • Kim, Seon-Bong (Department of Food Science and Technology/Institute of Food Science, Pukyong National University)
  • Received : 2014.04.23
  • Accepted : 2014.07.18
  • Published : 2014.09.30
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Abstract

The objective of this study was to elucidate the physicochemical characteristics of gelatin extracted from jellyfish Rhopilema hispidum. We investigated the proximate composition, amino acids, gel strength, gelling/melting points, dynamic viscoelastic properties, and viscosity of jellyfish gelatin. Jellyfish gelatin contained 12.2% moisture, 1.5% lipid, 2.1% ash, and 84.8% protein. Glycine, hydroxyproline, proline, and alanine were the predominant amino acids. The gelatin showed a gel strength of 31.2 kPa, a gelling point of $18.0^{\circ}C$, and melting point of $22.3^{\circ}C$. The gelatin was composed of ${\alpha}_1$-chain, ${\alpha}_2$-chain, ${\beta}$-chain, and ${\gamma}$-chain. During cooling and heating process, jellyfish gelatin showed lower elastic modulus (G') and loss modulus (G") values than mammalian gelatin. Jellyfish gelatin did not show superior rheological properties to mammalian gelatin, like other fish gelatin; however, it can be used in various food and cosmetic products not requiring high gel strength.

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References

  1. Arnesen JA and Gildberg A. 2002. Preparation and characterisation of gelatine from the skin of harp seal (Phoca groendlandica). Bioresour Technol 82, 191-194. https://doi.org/10.1016/S0960-8524(01)00164-X
  2. Association of Official Analytical Chemists (AOAC). 2006. Official methods of analysis of AOAC international (18th ed.). Virginia, USA: Association of Official and Analytical Chemists International.
  3. Avena-Bustillos RJ, Olsen CW, Olson DA, Chiou B, Yee E, Bechtel PJ and Mchugh TH. 2006. Water vapor permeability of mammalian and fish gelatin films. J Food Sci 71, 202-207. https://doi.org/10.1111/j.1750-3841.2006.00016.x
  4. Burjandze TV. 2000. New analysis of the phylogenetic change of collagen thermostability. Biopolymers 53, 523-528. https://doi.org/10.1002/(SICI)1097-0282(200005)53:6<523::AID-BIP8>3.0.CO;2-7
  5. Cho SM, Kwak KS, Park DC, Gu YS, Ji CI, Jang DH, Lee YB and Kim SB. 2004. Processing optimization and functional properties of gelatin from shark (Isurus oxyrinchus) cartilage. Food Hydrocoll 18, 573-579. https://doi.org/10.1016/j.foodhyd.2003.10.001
  6. Cho SM, Gu YS and Kim SB. 2005. Extracting optimization and physical properties of yellowfin tuna (Thunnus albacares) skin gelatin compared to mammalian gelatins. Food Hydrocoll 19, 221-229. https://doi.org/10.1016/j.foodhyd.2004.05.005
  7. Choi SS and Regenstein JM. 2000. Physicochemical and sensory characteristics of fish gelatin. J Food Sci 65, 194-199. https://doi.org/10.1111/j.1365-2621.2000.tb15978.x
  8. Gilsenan PM and Ross-Murphy SB. 2000. Rheological characterization of gelatins from mammalian and marine sources. Food Hydrocoll 14, 191-195. https://doi.org/10.1016/S0268-005X(99)00050-8
  9. Giraud-Guille MM, Besseau L, Chopin C, Durand P and Herbage D. 2000. Structural aspects of fish skin collagen which forms ordered arrays via liquid crystalline states. Biomaterials 21, 899-906. https://doi.org/10.1016/S0142-9612(99)00244-6
  10. Gomez-Guillen MC, Turnay J, Fernandez-Diaz MD, Ulmo N, Lizaebe MA and Montero P. 2002. Structural and physical properties of gelatin extracted from different marine species. Food Hydrocoll 16, 25-34. https://doi.org/10.1016/S0268-005X(01)00035-2
  11. Gudmundsson M. 2002. Rheological properties of fish gelatins. J Food Sci 67, 2172-2176. https://doi.org/10.1111/j.1365-2621.2002.tb09522.x
  12. Gudmundsson M and Hafsteinsson H. 1997. Gelatin from cod skins as affected by chemical treatment. J Food Sci 62, 37-39. https://doi.org/10.1111/j.1365-2621.1997.tb04363.x
  13. Haug IJ, Draget KI and Smidsrod O. 2004. Physical and rheological properties of fish gelatin compared to mammalian gelatin. Food Hydrocoll 18, 203-213. https://doi.org/10.1016/S0268-005X(03)00065-1
  14. Jamilah B and Harvinder KG. 2002. Properties of gelatins from skins of fish-black tilapia (Oreochromis mossambicus) and red tilapia (Oreochromis nilotica). Food Chem 77, 81-84. https://doi.org/10.1016/S0308-8146(01)00328-4
  15. Joly-Duhamel C, Hellio D, Ajdari A and Djabourov M. 2002. All gelatin networks: 2. The master curve for elasticity. Langmuir 18, 7158-7166. https://doi.org/10.1021/la020190m
  16. Kimura S, Zhu XP, Matsui R, Shijoh M and Takamizawa S. 1988. Characterization of fish muscle type I collagen. J Food Sci 53, 1315-1318. https://doi.org/10.1111/j.1365-2621.1988.tb09266.x
  17. Kittiphattanabawon P, Benjakul S, Visessanguan W, Nagai T and Tanaka M. 2005. Characerisation of acid-soluble collagen from skin and bond of bigeye snapper (Priacanthus tayenus). Food Chem 89, 363-372. https://doi.org/10.1016/j.foodchem.2004.02.042
  18. Kolodziejska I, Kaczorowski K, Piotrowska B and Sadowska M. 2004. Modification of the properties of gelatin from skins of Baltic cod (Gadus morhua) with transglutaminase. Food Chem 86, 203-209. https://doi.org/10.1016/j.foodchem.2003.08.036
  19. Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685. https://doi.org/10.1038/227680a0
  20. Ledward DA. 1986. Gelation of gelatin. In: Mitchell JR and Ledward DA, eds. Functional properties of food macromolecules. London: Elsevier Appl Sci Pub, pp. 171-201.
  21. Muyonga JH, Cole CGB and Duodu KG. 2004. Characterisation of acid soluble collagen from skins of young and adult Nile perch (Lates niloticus). Food Chem 85, 81-89. https://doi.org/10.1016/j.foodchem.2003.06.006
  22. Nagai T, Ogawa T, Nakamura T, Ito T, Nakagawa H, Fujiki K, Nakao M and Yano T. 1999. Collagen of edible jellyfish exumbrella. J Sci Food Agric 79, 855-858. https://doi.org/10.1002/(SICI)1097-0010(19990501)79:6<855::AID-JSFA299>3.0.CO;2-N
  23. Nagai T and Suzuki N. 2000. Isolation of collagen from fish waste material-skin, bone and fin. Food Chem 68, 277-281. https://doi.org/10.1016/S0308-8146(99)00188-0
  24. Nagai T and Suzuki N. 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
  25. Norland RE. 1987. Fish gelatin: technical aspects and applications. In: Band SJ ed., Photographic gelatin, Royal Photographic Society, London, pp. 266-281.
  26. Sarbon, N.M., Badii, F. and Howell, N.K. 2013. Preparation and characterisation of chicken skin gelatin as an alternative to mammalian gelatin. Food Hydrocoll 30, 143-151. https://doi.org/10.1016/j.foodhyd.2012.05.009
  27. Stainsby, G. 1987. In: A. M. Pearson, T. R. Dutson and A. J. Bailey, eds. Gelatin gels (Vol. 4) (pp. 209-222). Advances in meat research, collagen as a food, New York: Van Nostrand Reinhold.
  28. Winter HH and Chambon F. 1986. Analysis of linear viscoelasticity of a crosslinking polymer at the gel point. J Rheol 30, 367-382. https://doi.org/10.1122/1.549853