Thermal gelation of myofibrillar proteins from aquatic organisms

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

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

29 Scopus citations


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.

Translated title of the contributionGelificación térmica de proteínas miofibrilares de organismos acuáticos
Original languageEnglish
Pages (from-to)502-508
Number of pages7
JournalCYTA - Journal of Food
Issue number3
StatePublished - 2 Jul 2016

Bibliographical note

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


  • Protein gelation
  • myofibrillar proteins


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