Thermal gelation of myofibrillar proteins from aquatic organisms

Título traducido de la contribución: Gelificación térmica de proteínas miofibrilares de organismos acuáticos

I. J. Tolano-Villaverde, W. Torres-Arreola, V. M. Ocaño-Higuera, E. Marquez-Rios*

*Autor correspondiente de este trabajo

Producción científica: Contribución a una revistaArtículo de revisiónrevisión exhaustiva

29 Citas (Scopus)

Resumen

Gelling ability is attributed to myosin, which is the main myofibrillar protein. Therefore, its integrity is very important. However, a gel with good textural characteristics and stability depends on the inherent characteristics of its proteins, as well as on external factors (primarily temperature, pH, protein concentration and added salt). The best gels from aquatic organism proteins are obtained at a pH value of approximately 7.0. However, the concentration of salt is often variable. In contrast, when proteins are recovered using acid/alkaline dissolution, gels with good textural characteristics are obtained without salt. Hydrophobic interactions, disulfide bonds, hydrogen bonds, and electrostatic interactions are the main interactions that stabilize the protein gel. Thus, this review focuses on the study of the main factors involved in protein gelation, as well as on the extraction method effect on the gelling capacity of proteins from aquatic organisms.

Título traducido de la contribuciónGelificación térmica de proteínas miofibrilares de organismos acuáticos
Idioma originalInglés
Páginas (desde-hasta)502-508
Número de páginas7
PublicaciónCYTA - Journal of Food
Volumen14
N.º3
DOI
EstadoPublicada - 2 jul. 2016

Nota bibliográfica

Publisher Copyright:
© 2015 The Author(s). Published by Taylor & Francis.

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