Effect of acid treatment on extraction yield and gel strength of gelatin from whiptail stingray (Dasyatis brevis) skin

  • Marco Antonio Sántiz-Gómez
  • Miguel Angel Mazorra-Manzano
  • Hugo Enrique Ramírez-Guerra
  • Susana María Scheuren-Acevedo
  • Gerardo Navarro-García
  • Ramón Pacheco-Aguilar
  • Juan Carlos Ramírez-SuárezEmail author


Chemical properties of fish gelatins differ from those of conventional mammalian sources, representing an attractive technological alternative for the food industry. Ray filleting generates a considerable amount of skin waste that can be used as a collagen source for gelatin extraction. Thus, this research evaluated the HCl and CH3COOH effect, at 0.01, 0.025, 0.05, 0.075, 0.1, 0.15, and 0.2 M, on extraction yield, molecular weight distribution, and gel strength (GS) of whiptail stingray (Dasyatis brevis) skin gelatins. Results showed differences (P < 0.05) between acid type and concentration used. CH3COOH (0.15 M) gave the highest extraction yield (7.0% vs. 5.5% at 0.15 M HCl) and GS (653 ± 71 g vs. 619.5 ± 82 g at 0.2 M HCl). Gelatin electrophoretic profile from CH3COOH revealed α-/β-components and high molecular weight (> 200 kDa) polymers. Ray gelatin GS was higher than commercial bovine gelatin, suggesting its possible use for technological food applications.


Fish skin collagen Fish gelatin Acid treatment Gel strength Extraction yield 



Author Marco A. Sántiz-Gómez wishes to thank Consejo Nacional de Ciencia y Tecnología (CONACyT) of the Mexican Republic for the scholarship received during this research.


  1. AOAC. Official Methods of Analysis of AOAC International, 17th ed. Association of Official Analytical Chemists, Gaithersburg, MD, USA (2000)Google Scholar
  2. Bae I, Osatomi K, Yoshida A, Osako K, Yamaguchi A, Hara K. Biochemical properties of acid-soluble collagens extracted from the skins of underutilised fishes. Food Chem. 108(1): 49–54 (2008)CrossRefGoogle Scholar
  3. Bama P, Vijayalakshimi M, Jayasimman R, Kalaichelvan PT, Deccaraman M, Sankaranarayanan S. Extraction of collagen from cat fish (Tachysurus macalatus) by pepsin digestion and preparation and characterization of collagen chitosan sheet. Int. J. Pharm. Pharm. Sci. 2(4): 133–137 (2010)Google Scholar
  4. Binsi PK, Shamasundar BA, Dileep AO, Badii F, Howell NK. Rheological and functional properties of gelatin from the skin of Bigeye snapper (Priacanthus hamrur) fish: Influence of gelatin on the gel-forming ability of fish mince. Food Hydrocoll. 23(1): 132–145 (2009)CrossRefGoogle Scholar
  5. Bizzarro JJ, Smith WD, Márquez-Farías JF, Tyminski J, Hueter RE. Temporal variation in the artisanal elasmobranch fishery of Sonora, Mexico. Fish. Res. 97(1): 103–117 (2009)CrossRefGoogle Scholar
  6. Boran G, Regenstein JM. Optimization of gelatin extraction from silver carp skin. J. Food Sci. 74(8): 432–441 (2009)CrossRefGoogle Scholar
  7. Boran G, Regenstein JM. Fish gelatin. Vol. 60, pp. 119–143. In: Advances in Food and Nutrition Research. Steve LT (ed). Academic Press, New York, NY, USA (2010)Google Scholar
  8. Choi SS, Regenstein JM. Physicochemical and sensory characteristics of fish gelatin. J. Food Sci. 65(2): 194–199 (2000)CrossRefGoogle Scholar
  9. Gilsenan PM, Ross-Murphy SB. Rheological characterisation of gelatins from mammalian and marine sources. Food Hydrocoll. 14(3): 191–195 (2000)CrossRefGoogle Scholar
  10. GMIA. Standard testing methods for edible gelatin. Available from: Accessed 12 September 2018
  11. Gómez-Estaca J, Montero P, Fernández-Martín F, Gómez-Guillén MC. Physico-chemical and film-forming properties of bovine-hide and tuna-skin gelatin: a comparative study. J. Food Eng. 90: 480–486 (2009)CrossRefGoogle Scholar
  12. Gómez-Guillén MC, Montero P. Extraction of gelatin from megrim (Lepidorhombus boscii) skins with several organic acids. J. Food Sci. 66(2): 213–216 (2001)CrossRefGoogle Scholar
  13. Gómez-Guillén MC, Turnay J, Fernández-Díaz MD, Ulmo N, Lizarbe MA, Montero P. Structural and physical properties of gelatin extracted from different marine species: a comparative study. Food Hydrocoll. 16(1): 25–34 (2002)CrossRefGoogle Scholar
  14. Gómez-Guillén MC, Pérez-Mateos M, Gómez-Estaca E, López-Caballero E, Giménez B, Montero P. Fish gelatin: a renewable material for developing active biodegradable films. Trends Food Sci. Technol. 20: 3–16 (2009)CrossRefGoogle Scholar
  15. Gómez-Guillén MC, Giménez B, López-Caballero ME, Montero MP. Functional and bioactive properties of collagen and gelatin from alternative sources: a review. Food Hydrocoll. 25(8): 1813–1827 (2011)CrossRefGoogle Scholar
  16. Gornall AG, Bardawill CJ, David MM. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177(2): 751–766 (1949)PubMedGoogle Scholar
  17. Haug IJ, Draget KI. Gelatin. pp. 142–163. In: Handbook of Hydrocolloids. Phillips GO, Williams PA (eds). Woodhead Publishing, Cambridge, England (2009)CrossRefGoogle Scholar
  18. Haug IJ, Draget KI, Smidsrød O. Physical and rheological properties of fish gelatin compared to mammalian gelatin. Food Hydrocoll. 18(2): 203–213 (2004)CrossRefGoogle Scholar
  19. Huss HH. Fresh Fish—Quality and Quality Changes. Food and Agriculture Organization of the United Nations, Rome (1988)Google Scholar
  20. Jamilah B, Harvinder KG. Properties of gelatins from skins of fish—black tilapia (Oreochromis mossambicus) and red tilapia (Oreochromis nilotica). Food Chem. 77(1): 81–84 (2002)CrossRefGoogle Scholar
  21. Jellouli K, Balti R, Bougatef A, Hmidet N, Barkia A, Nasri M. Chemical composition and characteristics of skin gelatin from grey triggerfish (Balistes capriscus). LWT—Food Sci. Technol. 44(9): 1965–1970 (2011)CrossRefGoogle Scholar
  22. Karim AA, Bhat R. Gelatin alternatives for the food industry: recent developments, challenges and prospects. Trends Food Sci. Technol. 19: 644–656 (2008)CrossRefGoogle Scholar
  23. Karim AA, Bhat R. Fish gelatin: properties, challenges, and prospects as an alternative to mammalian gelatins. Food Hydrocoll. 23: 563–576 (2009)CrossRefGoogle Scholar
  24. Kim JS, Park JW. Characterization of acid-soluble collagen from Pacific whiting surimi processing byproducts. J. Food Sci. 69(8): 637–642 (2004)CrossRefGoogle Scholar
  25. Kittiphattanabawon P, Benjakul S, Visessanguan W, Shahidi F. Comparative study on characteristics of gelatin from the skins of brownbanded bamboo shark and blacktip shark as affected by extraction conditions. Food Hydrocoll. 24(2): 164–171 (2010a)CrossRefGoogle Scholar
  26. Kittiphattanabawon P, Benjakul S, Visessanguan W, Shahidi F. Isolation and properties of acid- and pepsin-soluble collagen from the skin of blacktip shark (Carcharhinus limbatus). Eur. Food Res. Technol. 230: 475–483 (2010b)CrossRefGoogle Scholar
  27. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685 (1970)CrossRefGoogle Scholar
  28. Lassoued I, Jridi M, Nasri R, Dammak A, Hajji M, Nasri M, Barkia A. Characteristics and functional properties of gelatin from thornback ray skin obtained by pepsin-aided process in comparison with commercial halal bovine gelatin. Food Hydrocoll. 41: 309–318 (2014)CrossRefGoogle Scholar
  29. Leuenberger BH. Investigation of viscosity and gelation properties of different mammalian and fish gelatins. Food Hydrocoll. 5(4): 353–361 (1991)CrossRefGoogle Scholar
  30. Muyonga JH, Cole CGB, Duodu KG. Extraction and physico-chemical characterisation of Nile perch (Lates niloticus) skin and bone gelatin. Food Hydrocoll. 18(4): 581–592 (2004)CrossRefGoogle Scholar
  31. Schrieber R, Gareis H. From collagen to gelatine. pp. 45–117. In: Gelatine Handbook. Theory and Industrial Practice. Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany (2007)CrossRefGoogle Scholar
  32. See SF, Ghassem M, Mamot S, Babji AS. Effect of different pretreatments on functional properties of African catfish (Clarias gariepinus) skin gelatin. J. Food Sci. Technol. 52(2): 753–762 (2015)CrossRefGoogle Scholar
  33. Tabarestani HS, Maghsoudlou Y, Motamedzadegan A, Sadeghi Mahoonak AR. Optimization of physico-chemical properties of gelatin extracted from fish skin of rainbow trout (Onchorhynchus mykiss). Bioresour. Technol. 101(15): 6207–6214 (2010)CrossRefGoogle Scholar
  34. Wang C, Chang T, Shi L, Yang H, Cui M, Tambalu L. Seafood processing by-products: collagen and gelatin. pp. 207–242. In: Seafood Processing By-Products. Trends and Applications. Kim S-K (ed). Springer, New York, NY, USA (2014)CrossRefGoogle Scholar
  35. Zeng S, Yan X, Cao W, Hong P, Zhang C, Li L. Optimisation of extraction conditions and characteristics of skin gelatin from Nile tilapia (Oreochromis niloticus). Int. J. Food Sci. Technol. 45(9): 1807–1813 (2010)CrossRefGoogle Scholar
  36. Zhou P, Regenstein JM. Effects of alkaline and acid pretreatments on Alaska pollock skin gelatin extraction. J. Food Sci. 70(6): C392–C396 (2005)CrossRefGoogle Scholar
  37. Zhou P, Mulvaney SJ, Regenstein JM. Properties of Alaska pollock skin gelatin: a comparison with tilapia and pork skin gelatins. J. Food Sci. 71(6): C313–C321 (2006)CrossRefGoogle Scholar

Copyright information

© The Korean Society of Food Science and Technology and Springer Science+Business Media B.V., part of Springer Nature 2018

Authors and Affiliations

  • Marco Antonio Sántiz-Gómez
    • 1
  • Miguel Angel Mazorra-Manzano
    • 1
  • Hugo Enrique Ramírez-Guerra
    • 1
  • Susana María Scheuren-Acevedo
    • 1
  • Gerardo Navarro-García
    • 2
  • Ramón Pacheco-Aguilar
    • 1
  • Juan Carlos Ramírez-Suárez
    • 1
    Email author
  1. 1.Centro de Investigación en Alimentación y DesarrolloHermosilloMexico
  2. 2.Departamento de Investigaciones Científicas y TecnológicasUniversidad de SonoraHermosilloMexico

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