Skip to main content
SpringerLink
Log in

Thermal characteristics of gelatin extracted from shaari fish skin

Effects of extraction conditions

  • Published:
Journal of Thermal Analysis and Calorimetry Aims and scope Submit manuscript

Abstract

Gelatin extraction yield increased with the increase of acetic acid concentration and temperature. Gelatin extracted from shaari skin using 0.1 N acid solutions and temperatures of 323 and 353 K gave highest protein content comparable to that of commercial bovine and porcine gelatins. In general, gelatin extracted from shaari gelatin showed lower onset of glass transition temperature than mammalian gelatins. For shaari skin gelatin, the onset of glass transition temperature decreased with the increase of extraction temperature up to 323 K and then remained nearly constant. The decrease in glass transition was more pronounced for gelatin extracted at 0.01 N compared to the 0.1 and 1.0 N samples. Unfolding temperature decreased exponentially with the increase of extraction temperature. The unfolding temperature shifted to lower temperature, and the decrease was more pronounced in the case of higher (1.0 N) concentrated samples. The extraction concentration and temperature did not show significant effect on the onset solids-melting temperature.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2

Similar content being viewed by others

Abbreviations

T gi :

Onset temperature of glass transition (K)

T gp :

Peak temperature of glass transition (K)

T ge :

End temperature of glass transition (K)

T mi :

Onset temperature of solids-melting (K)

T mm :

Maximum slope temperature of solids-melting (K)

T mp :

Peak temperature of solids-melting (K)

T me :

End temperature of solids-melting (K)

T ui :

Onset unfolding temperature (K)

T um :

Maximum slope of unfolding temperature (K)

T up :

Peak of unfolding temperature (K)

X w :

Moisture content (g/100 g sample)

ΔC p :

Change of specific heat (J/kg K)

ΔH u :

Enthalpy change for unfolding (kJ/kg)

ΔH m :

Enthalpy change for solids-melting (kJ/kg)

References

  1. Karim AA, Bhat R. Gelatin alternatives for the food industry: recent developments, challenges and prospects. Trends Food Sci Technol. 2008;19(12):644–56.

    Article  CAS  Google Scholar 

  2. Montero P, Gómez-Guillén MC. Extracting conditions for megrim (Lepidorhombus boscii) skin collagen affect functional properties of the resulting gelatin. J Food Sci. 2000;65:434–8.

    Article  CAS  Google Scholar 

  3. Wainewright FW. Physical tests for gelatin and gelatin products. In: Ward AG, Courts A, editors. The science and technology of gelatin. New York: Academic Press; 1977. p. 507–34.

    Google Scholar 

  4. Hinterwaldner R. Raw material. In: Ward AG, Courts A, editors. The science and technology of gelatin. New York: Academic Press; 1977. p. 295–314.

    Google Scholar 

  5. Gennadios A, McHugh TH, Weller CL, Krochta JM. Edible coatings and films based on proteins. In: Krochta JM, Baldwin EA, Nisperos-Carriedo M, editors. Edible coatings and films to improve food quality. Lancaster: Technomic Publishing Company; 1994. p. 201–78.

    Google Scholar 

  6. Slade L, Levine H. Polymer-chemical properties of gelatin in foods. In: Pearson AM, Dutson TR, Bailey AJ, editors. Collagen as food: vol 4. Advances in meat research, vol. 4. New York: Van Nostrand Reinhold; 1987. p. 251–66.

    Google Scholar 

  7. Haug IJ, Draget KI, Smidsrod O. Physical and rheological properties of fish gelatin compared to mammalian gelatin. Food Hydrocoll. 2004;18:203–13.

    Article  CAS  Google Scholar 

  8. Leuenberger BH. Investigation of viscosity and gelation properties of different mammalian and fish gelatins. Food Hydrocoll. 1991;54:353–61.

    Article  Google Scholar 

  9. Zhang S, Wang Y, Herring JL, Oh JH. Characterization of edible film fabricated with channel catfish (Ictalurus punctatus) gelatin extract using selected pretreatment methods. J Food Sci. 2007;72(9):C498–503.

    Article  CAS  Google Scholar 

  10. Yang H, Wang Y, Zhou P, Regenstein JM. Effects of alkaline and acid pretreatment on the physical properties and nanostructures of the gelatin from channel catfish skins. Food Hydrocoll. 2008;22:1541–50.

    Article  CAS  Google Scholar 

  11. Zhou P, Regenstein JM. Optimization of extraction conditions for Pollock skin gelatin. J Food Sci. 2004;69(5):C393–8.

    CAS  Google Scholar 

  12. Rahman MS. State diagram of date flesh using differential scanning calorimetry (DSC). Int J Food Prop. 2004;7(3):407–28.

    Article  Google Scholar 

  13. Rahman MS. State diagram of foods: its potential use in food processing and product stability. Trends Food Sci Technol. 2006;17:129–41.

    Article  CAS  Google Scholar 

  14. Rahman MS. Food stability beyond water activity and glass transition: macro-micro region concept in the state diagram. Int J Food Prop. 2009;12(4):726–40.

    Article  CAS  Google Scholar 

  15. D’Cruzand NM, Bell LN. Thermal unfolding of gelatin in solids as affected by the glass transition. J Food Sci. 2005;70(2):E64–8.

    Article  Google Scholar 

  16. Bell L, Touma DE. Glass transition temperatures determined using a temperature-cycling differential scanning calorimetry. J Food Sci. 1996;61(4):807–28.

    Article  CAS  Google Scholar 

  17. Marshall AS, Petrie SEB. Thermal transitions in gelatin and aqueous gelatin solutions. J Photogr Sci. 1980;28:128–34.

    CAS  Google Scholar 

  18. Sablani SS, Kasapis S, Al-Rahbi Y, Al-Mugheiry M. Water sorption isotherms and glass transition properties of gelatin. Dry Technol. 2002;20(10):2081–92.

    Article  CAS  Google Scholar 

  19. Sobral PJA, Habitante AMQB. Phase transitions of pigskin gelatin. Food Hydrocoll. 2001;15:377–82.

    Article  CAS  Google Scholar 

  20. Vanin FM, Sobral PJA, Menegalli FC, Carvalho RA, Habitante AMQB. Effects of plasticizers and their concentrations on thermal and functional properties of gelatin-based films. Food Hydrocoll. 2005;19:899–907.

    Article  CAS  Google Scholar 

  21. Rahman MS, Al-Saidi GS, Guizani N. Thermal characterization of gelatin extracted from yellowfin tuna skin and commercial mammalian gelatin. Food Chem. 2008;108:472–81.

    Article  CAS  Google Scholar 

  22. Gomez-Guillen M, Montero P. Method for the production of gelatin of marine origin and product thus obtained. International Patent PCT/S01/00275. 2001.

  23. AOAC. Official methods of analysis. 15th ed. Washington, DC: Association of Official Analytical Chemists; 1990.

    Google Scholar 

  24. Pico-Tag. Amino acid analysis system. Midford: Waters Corporation; 1984.

    Google Scholar 

  25. Rahman MS, Al-Mahrouqi AI. Instrumental texture profile analysis of gelatin gel extracted from grouper skin and commercial (bovine and porcine) gelatin gels. Int J Food Sci Nutr. 2009;60(S7):229–42.

    Article  Google Scholar 

  26. Gudmundsson M, Hafsteinsson H. Gelatin from cod skins as affected by chemical treatments. J Food Sci. 1997;62:37–47.

    Article  CAS  Google Scholar 

  27. Jamilah B, Harvinder KG. Properties of gelatins from skins of fish-black tilapia (Oreochromis mossambicus) and red tilapia (Oreochromis nilotica). Food Chem. 2002;77:81–4.

    Article  CAS  Google Scholar 

  28. Gomez-Guillen MC, Turnay J, Fernandez-Diaz MD, Ulmo N, Lizarbe MA, Montero P. Structural and physical properties of gelatin extracted from different marine species: a comparative study. Food Hydrocoll. 2002;16:25–34.

    Article  CAS  Google Scholar 

  29. Mizuta S, Yoshinaka R, Sato M, Sakaguchi M. Hot-water solubility of collagen from the muscle of kuruma prawn. Fisheries Sci. 1995;61:536–7.

    CAS  Google Scholar 

  30. Peterson BR, Yates JR. Gelatin extraction. United-States-Patent. 4 064 008. Novo Industri AS. 1977.

  31. Eysturskaro J, Haug IJ, Elharfaoui N, Djabourov M, Draget KI. Structural and mechanical properties of fish gelatin as a function of extraction conditions. Food Hydrocoll. 2009;23:1702–11.

    Article  Google Scholar 

  32. Djabourov M, Lechaire J, Gaill F. Structure and rheology of gelatin and collagen gels. Biorheology. 1993;30:191–205.

    CAS  Google Scholar 

  33. De Batista TM, Martins VCA, De Guzzi Plepis AM. Thermal behavior of in vitro mineralized anionic collagen matrices. J Therm Anal Calorim. 2009;95(3):945–9.

    Article  CAS  Google Scholar 

  34. Joly-Duhamel C, Hellio D, Djabourov M. All gelatin networks: 1. Biodiversity and physical chemistry. Langmuir. 2002;18:7208–17.

    Article  CAS  Google Scholar 

  35. Arnesen JA, Gildberg A. Extraction and characterisation of gelatine from Atlantic salmon (Salmo salar) skin. Bioresour Technol. 2007;98:53–7.

    Article  CAS  Google Scholar 

  36. Zhou P, Regenstein JM. Effects of Alkaline and acid pretreatments on Alask Pollock skin gelatin extraction. J Food Sci. 2005;70(6):C392–6.

    Article  CAS  Google Scholar 

  37. Balian G, Bowes JH. The structure and properties of collagen. In: Ward AG, Courts A, editors. The science and technology of gelatin. New York: Academic Press; 1977. p. 1–31.

    Google Scholar 

  38. Rother J. Edible gelatin types, properties, use and application in the food industry. Food Tech Europe. 1995;1(5):32–42.

    Google Scholar 

  39. Sarabia AI, Gomez-Guillen MC, Montero P. The effect of added salts on the viscoelastic properties of fish skin gelatin. Food Chem. 2000;70:71–6.

    Article  CAS  Google Scholar 

  40. Arnesen JA, Gildberg A. Preparation and characterisation of gelatine from the skin of harp seal (Phoca groenlandica). Bioresour Technol. 2002;82:191–4.

    Article  CAS  Google Scholar 

  41. Badii F, Howell NK. Fish gelatin: structure, gelling properties and interaction with egg albumen proteins. Food Hydrocoll. 2006;20:630–40.

    Article  CAS  Google Scholar 

  42. Johnston-Banks FA. Gelatin. In: Harris P, editor. Food gels. London: Elsevier Applied Science Publ; 1990. p. 233–89.

    Google Scholar 

  43. Ledward DA. Gelation of gelatin. In: Mitchell JR, Ledward DA, editors. Functional properties of food macromolecules. London: Elsevier Applied Science Publ; 1986. p. 171–201.

    Google Scholar 

  44. Burjandze TV. Hydroxy-proline content and location in relation to collagen thermal stability. Biopolymers. 1979;18:931–6.

    Article  Google Scholar 

  45. Mizuno K, Hayashi T, Bachinger HP. Hydroxylation-induced stabilization of the collagen triple helix. Further characterization of peptides with 4(R)-hydroxyproline in the Xaa position. J Biol Chem. 2003;278:32373–9.

    Article  CAS  Google Scholar 

  46. Badea E, Miu L, Budrugeac P, Giurginca M, Masic A, Badea N, Gatta GD. Study of deterioration of historical parchments by various thermal analysis techniques complemented by SEM, FTIR, UV–VIS–NIR and unilateral NMR Investigations. J Therm Anal Calorim. 2008;91:17–27.

    Article  CAS  Google Scholar 

  47. Norland RE. Fish gelatin technical aspects and applications. In: Bland SJ, editor. Photographic gelatin. London: Royal Photographic Society; 1987. p. 266–81.

    Google Scholar 

  48. Gilsenan PM, Ross-Murphy SB. Rheological characterization of gelatins from mammalian and marine sources. Food Hydrocoll. 2000;14:191–5.

    Article  CAS  Google Scholar 

  49. Anker M, Stading M, Hermansson A. Effects of pH and gel state on the mechanical properties, moisture contents, and glass transition temperatures of whey protein films. J Agric Food Chem. 1999;47:1878–86.

    Article  CAS  Google Scholar 

  50. Gimenez B, Turnay J, Lizarbe MA, Montero P, Gómez-Guillén MC. Use of lactic acid for extraction of fish skin gelatin. Food Hydrocoll. 2005;19:941–50.

    Article  CAS  Google Scholar 

  51. Asghar A, Henrickson RL. Chemical, biochemical, functional, and nutritional characteristics of collagen in food system. Adv Food Res. 1982;28:231–372.

    CAS  Google Scholar 

Download references

Acknowledgements

The authors would like to acknowledge the support of Sultan Qaboos University toward this research in developing fish skin gelatin. Mr. Ghalib Al-Saidi has been awarded a Ph. D. scholarship from Sultan Qaboos University.

Author information

Authors and Affiliations

  1. Department of Food Science and Nutrition, College of Agricultural and Marine Sciences, Sultan Qaboos University, P. O. Box 34, Al-Khod-123, Muscat, Oman

    Ghalib Al-Saidi, Mohammad Shafiur Rahman, Ahmed Al-Alawi & Nejib Guizani

Authors
  1. Ghalib Al-Saidi
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Mohammad Shafiur Rahman
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Ahmed Al-Alawi
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Nejib Guizani
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Mohammad Shafiur Rahman.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Al-Saidi, G., Rahman, M.S., Al-Alawi, A. et al. Thermal characteristics of gelatin extracted from shaari fish skin. J Therm Anal Calorim 104, 593–603 (2011). https://doi.org/10.1007/s10973-010-1240-8

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10973-010-1240-8

Keywords

Search

Navigation