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     Advance Journal of Food Science and Technology


Obtaining Gelatin from the Skin of Gilthead Bream (Brachyplathystomarousseauxii) using Two Pre-treatment

1Elen Vanessa Costa da Silva, 2Lucia de Fatima Henriques Lourenco and 3Rosinelson da Silva Pena
1Food Technology Department, Estadual University of Pará, UEPA, Postal Code: 66095-015
2Faculty of Food Engineering,
3Faculty of Food Engineering, Technology Institute, Federal University of Pará (UFPA), Rua Augusto Côrrea, 01, P.O. Box 479, Postal code: 66075-110, Belém, PA, Brazil
Advance Journal of Food Science and Technology  2017  5:182-189
http://dx.doi.org/10.19026/ajfst.13.5067  |  © The Author(s) 2017
Received: March 14, 2017  |  Accepted: June 3, 2017  |  Published: July 25, 2017

Abstract

Different pre-treatment and extraction processes have been researched to provide information on the properties of gelatin from fish skin and conversion rate of collagen into gelatin.Two methodologies were employed to extract collagen and obtain gelatin from the skin of gilthead bream (Brachyplathystomarousseauxii). Pre-treatment with sodium hydroxide (NaOH) and calcium hydroxide (Ca(OH)2) was used and the gelatin obtained was characterized through analyses of yield, gel strength, color, viscosity, amino acid profile, melting point, emulsifying capacity and scanning electron microscopy. Both gelatins were classified as type A, which is attributed to the chemical treatment with acid employed in the collagen pre-treatment step. When the characteristics of the gelatins obtained were compared, the one that used NaOH had greater (p<0.05) technological potential due to higher yield, greater amount of imino acids and better properties (gel strength, viscosity, melting point, emulsifying power). However, the gelatin extracted with Ca(OH)2 had weak gels and lower melting point, which is appropriate for refrigerated products that require low gelling temperatures. When gelatins obtained with NaOH and Ca(OH)2were compared, the structure of the former has more empty protein filaments possibly correlated with the low aggregation of peptide chains during gelling It is concluded that the two gelatins obtained can be used in several applications in products according with the characteristic desired.

Keywords:

Collagen, fish, gel strength, hydroxyproline, residue,


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Competing interests

The authors have no competing interests.

Open Access Policy

This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

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The authors have no competing interests.

ISSN (Online):  2042-4876
ISSN (Print):   2042-4868
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