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Food Hydrocolloids
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Food Hydrocolloids
Article . 2018 . Peer-reviewed
License: Elsevier TDM
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Protein aggregation, water binding and thermal gelation of salt-ground hake muscle in the presence of wet and dried soy phosphatidylcholine liposomes

Authors: Marín, Daniel; Alemán, Ailén; Montero García, Pilar; Gómez Guillén, M. C.;

Protein aggregation, water binding and thermal gelation of salt-ground hake muscle in the presence of wet and dried soy phosphatidylcholine liposomes

Abstract

Different soy phosphatidylcholine liposomal preparations (fresh, high-pressure-treated, frozen-thawed, freeze-dried and spray-dried) were incorporated in salt-ground hake (M. merluccius) muscle and their effects on protein aggregation, water binding and thermal gelation were studied. Hydrodynamic properties of liposomes varied within the range of 123–507 nm for particle size and −40 to −49.5 mV for zeta potential. Addition of liposomes to the salt-ground muscle decreased protein solubility and increased water holding capacity, regardless of the vesicle particle size or membrane surface charge. Liposomes caused an increase in protein thermal stability, as observed by DSC, and also increased the spacing between myofibrils, leading to more water trapped within the myofibrillar protein network, as revealed by the LF-NMR-H study. The presence of liposomes slightly modified the viscoelastic behaviour and interfered with the thermal aggregation of muscle proteins, the mechanisms for this interference being different depending on the type of liposome preparation (wet or dry form). The present work suggests the possible use of a highly appreciated fish species, which could be subjected to landing obligation under Total Allowable Catch regulations (EU), for the development of a high-added-value fish product functionalized by the addition of liposomes.

The authors wish to thank the Spanish Ministry of Economy and Competitiveness (MINECO) for financial support (project AGL2014-52825 and AGL2017-84161-C2-1-R).

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Keywords

Hake mince, Thermal gelation, Soy phosphatidylcholine, Water binding, Protein aggregation, Dried liposomes

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
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