Behaviour of liposomes under various technological treatments in the gelling properties of hake muscle
The objective of this study is to evaluate the behaviour of the addition of nano-vesicles in the gelation of hake muscle, as a matrix to develop gel-like functional foods. Nano-vesicles elaborated from phosphatidylcholine were subjected to different technological treatments such as high pressure (600MPa), freezing, freeze-drying and spray drying and then they were incorporated into hake mince. The liposome (141 nm) wasn´t change by high pressure (HP) while the addition of glycerol as cryo-protector modified the final size of liposome depending of the treatment applied (freezing or freeze-drying). On the other hand, the atomized liposome by spray-dry offered a rentable alternative to the lyophilization process. All liposomes maintained a very electronegative zeta-potential (-39.6 to -49.5 mV) indicative of their high stability. In the relaxometry T2 analyzed by low-field nuclear magnetic resonance (LF-NMR) of the batters (salt-ground muscle formulations) it is observed that the liposome-containing batters showed more water binding capacity than the control batter without liposomes, contributing to maintain the hydrated structure of the myofibrillar protein. The temperature sweep rheological test reflected that the liposomes didn´t affect negatively the thermal gelation of the muscle, and the frequency sweep test that they increased the fluidity of the corresponding liposome-containing batters by inducing less protein-protein interaction. It is in agreement with the gel strength, which shown a higher value for control gels both 60 as 80 °C, indicating a higher protein aggregation than in liposome-containing batters. In summary, the addition of liposomes improved the structure and organization of the hake mince matrix.
| Main Authors: | , , , |
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| Format: | comunicación de congreso biblioteca |
| Language: | Spanish / Castilian |
| Published: |
2017
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| Subjects: | Phosphatidylcholine, Liposomes, Glycerol, Hake mince, Protein aggregation, |
| Online Access: | http://hdl.handle.net/10261/175687 |
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