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Kolotova, D., & Petrova, L. (2020). Technology and Physico-chemical Properties of Gelatin from Atlantic Cod Skin. KnE Life Sciences, 5(1), 426–436. https://doi.org/10.18502/kls.v5i1.6101

https://doi.org/10.18502/kls.v5i1.6101

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authors

  • Daria Kolotova

    Daria Kolotova

    Department of Chemistry, Murmansk State Technical University, Murmansk, Russia
  • Lyudmila Petrova

    Lyudmila Petrova

    Department of Chemistry, Murmansk State Technical University, Murmansk, Russia

Published Date

  • Jan 15, 2020

Technology and Physico-chemical Properties of Gelatin from Atlantic Cod Skin

KnE Life Sciences / International Applied Research Conference «Biological Resources Development and Environmental Management» / Pages 426–436

Abstract

In this work, the technology of fish gelatin from the skin of Atlantic cod from the Barents Sea was developed. The influence of enzyme type, extraction time, and pH of extraction on properties of fish gelatin was studied. The usage of proteolytic enzymes increases the yield of gelatin in comparison with acidic treatment, but the molecular weight of gelatin and viscosity of its solution decrease. The results observed related to the cleavage of peptide bonds of collagen during the enzymolysis process. The increase the time of extraction leads to an increase in molecular weight and quality of gelatin obtained. It was shown that gelatin obtained can be successfully used in the production of functional food products based on fish raw materials. The results obtained are of great importance for the fish-processing industry. They allow transforming existing technologies into non-waste processes and thereby enhance the effectiveness of enterprises and create better environmental conditions.

References
[1] Cai, L., Feng, J., Regenstein, J., et al. (2017). Confectionery gels: Effects of low calorie sweeteners on the rheological properties and microstructure of fish gelatin. Food Hydrocolloids, vol. 67, pp. 157–165.

[2] Gomez-Guillen, M. C., Gimenez, B., Lopez-Caballero, M. E., Montero, M. P. (2011). Functional and bioactive properties of collagen and gelatin from alternative sources: A review. Food hydrocolloids, vol. 25, pp. 1813–1827.

[3] Veis, A. (1964). The Macromolecular Chemistry of Gelatin. New York, London: Academic Press.

[4] Brewer, M.S. (2001). Bovine spongiform encephalopathy — Food safety implications. Advances in Food and Nutrition Research, vol. 43, pp. 265–317.

[5] Gomez-Guillen, M. C., Gimenez, B., Lopez-Caballero, M. E., Montero, M. P. (2011). Functional and bioactive properties of collagen and gelatin from alternative sources: A review. Food hydrocolloids, vol. 25, pp. 1813–1827.

[6] Alemán, A. et al. (2011). Enzymatic hydrolysis of fish gelatin under high pressure treatment. International Journal of Food Science & Technology, vol. 46, pp. 1129–1136.

[7] Kołodziejska, I. et al. (2004). Modification of the properties of gelatin from skins of Baltic cod (Gadus morhua) with transglutaminase. Food Chemistry, vol. 86, pp. 203–209.

[8] GOST 11293–89. Gelatin. Technical specification]. Moscow, Standartinform Publ., 1989. 24 p. (in Russian)

[9] Prystupa, D.A., Donald, A.M. (1996). Infrared study of gelatin conformations in the gel and sol states. Polymer Gels and Networks, vol. 4, pp. 87–110.

[10] Muyonga, J.H., Cole, C.G.B, Duodu, K.G. (2004). Fourier transform infrared (FTIR) spectroscopic study of acid soluble collagen and gelatin from skins and bones of young and adult Nile perch. Food Chemistry, vol. 86, pp. 325–332.