2024-03-29T02:19:18Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/1797492020-01-28T08:37:37Zcom_10261_70com_10261_2col_10261_323
Marín, Daniel
Alemán, Ailén
Montero García, Pilar
Gómez Guillén, M. C.
2019-04-10T07:12:02Z
2019-04-10T07:12:02Z
2018
LWT 98: 46-53 (2018)
0023-6438
http://hdl.handle.net/10261/179749
10.1016/j.lwt.2018.08.018
http://dx.doi.org/10.13039/501100003329
Soy phosphatidylcholine liposomes made with addition of trehalose as cryoprotectant were subjected to freeze-thawing and freeze-drying treatments, and subsequently incorporated in salt-ground hake (M. merluccius) muscle to study their effects on protein aggregation, water binding and thermal gelation. Both liposomal preparations presented similar particle size (≈215 nm, expressed as z-average) and strong electronegative zeta potential (−46 mV). The addition of both types of liposomal preparations led to more water trapped within the myofibrillar protein in the salt-ground muscle, as observed by water holding capacity (WHC) and low field nuclear magnetic resonance (LF-NMR). However, the liposomes interfered strongly with the thermal gelation ability of the muscle protein. Differential scanning calorimetry (DSC) analysis of the salt-ground muscle showed that the liposomes caused an increase in the main transition temperature associated with the actin molecule, with a concomitant reduction in total enthalpy change. The hydration state of the trehalose-containing liposomes did not play a significant role in textural properties of the resulting gels. The detrimental role of liposomes in the texture of fish gels should be considered in the design of functional fish products.
eng
openAccess
Hake muscle
Liposomes
Trehalose
Water binding
Thermal gelation
Gelling properties of hake muscle with addition of freeze-thawed and freeze-dried soy phosphatidylcholine liposomes protected with trehalose
artículo