Proteomic identification and physicochemical characterisation of paramyosin and collagen from octopus (Octopus vulgaris) and jumbo squid (Dosidicus gigas)

Summary To perform improvements in food science, it is fundamental to understand the physicochemical properties of proteins since their interaction with other macromolecules plays an essential role in food systems. Collagen and paramyosin help in the maintenance of the matrix structure cells, the te...

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Published inInternational journal of food science & technology Vol. 55; no. 10; pp. 3246 - 3253
Main Authors Tapia‐Vasquez, Angel Edgardo, Ezquerra‐Brauer, Josafat Marina, Márquez‐Ríos, Enrique, Ramírez‐Suárez, Juan Carlos, Huerta‐Ocampo, José Ángel, Santacruz‐Ortega, Hisila, Torres‐Arreola, Wilfrido
Format Journal Article
LanguageEnglish
Published Oxford Wiley Subscription Services, Inc 01.10.2020
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Summary:Summary To perform improvements in food science, it is fundamental to understand the physicochemical properties of proteins since their interaction with other macromolecules plays an essential role in food systems. Collagen and paramyosin help in the maintenance of the matrix structure cells, the textural behaviour and the technical functionality of the protein concentrates; because of this, their identification and characterisation are necessary. Cephalopods species have shown differences in the distribution of its muscle fibres. The amino acid profile of jumbo squid showed a high content of glycine and hydroxyproline, while octopus showed a high content of acidic amino acids. The thermal profile of jumbo squid showed an endothermic transition at 117 °C, which octopus did not present. Moreover, the proteomic identification confirms the identity of paramyosin with 33% coverage to paramyosin from Dosidicus gigas and a 4% coverage to collagen type II from Sepia pharaonis on octopus and jumbo squid, respectively. After an acidic extraction of proteins from octopus (Octopus vulgaris) and jumbo squid (Dosidicus gigas) the proteomic identification and physicochemical characterisation confirms the identity of paramyosin and collagen.
ISSN:0950-5423
1365-2621
DOI:10.1111/ijfs.14587