Thermal gelation of myofibrillar proteins from aquatic organisms

Research output: Contribution to journalScientific reviewpeer-review

19 Scopus citations


© 2015 The Author(s). Published by Taylor & Francis. 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.
Original languageAmerican English
Pages (from-to)502-508
Number of pages7
JournalCYTA - Journal of Food
StatePublished - 2 Jul 2016


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