Role of lipid phase separations and membrane hydration in phospholipid vesicle fusion

Biochemistry ◽  
1982 ◽  
Vol 21 (12) ◽  
pp. 2833-2840 ◽  
Author(s):  
Dick Hoekstra
Gels ◽  
2021 ◽  
Vol 7 (2) ◽  
pp. 48
Author(s):  
Ana M. Herrero ◽  
Claudia Ruiz-Capillas

Considerable attention has been paid to emulsion gels (EGs) in recent years due to their interesting applications in food. The aim of this work is to shed light on the role played by chia oil in the technological and structural properties of EGs made from soy protein isolates (SPI) and alginate. Two systems were studied: oil-free SPI gels (SPI/G) and the corresponding SPI EGs (SPI/EG) that contain chia oil. The proximate composition, technological properties (syneresis, pH, color and texture) and structural properties using Raman spectroscopy were determined for SPI/G and SPI/EG. No noticeable (p > 0.05) syneresis was observed in either sample. The pH values were similar (p > 0.05) for SPI/G and SPI/EG, but their texture and color differed significantly depending on the presence of chia oil. SPI/EG featured significantly lower redness and more lightness and yellowness and exhibited greater puncture and gel strengths than SPI/G. Raman spectroscopy revealed significant changes in the protein secondary structure, i.e., higher (p < 0.05) α-helix and lower (p < 0.05) β-sheet, turn and unordered structures, after the incorporation of chia oil to form the corresponding SPI/EG. Apparently, there is a correlation between these structural changes and the textural modifications observed.


FEBS Letters ◽  
1989 ◽  
Vol 257 (2) ◽  
pp. 447-450 ◽  
Author(s):  
D. Massotte ◽  
F. Pattus

1974 ◽  
Vol 2 (5-6) ◽  
pp. 609-616 ◽  
Author(s):  
W. Kleemann ◽  
C. W. M. Grant ◽  
H. M. McConnell

2018 ◽  
Vol 430 (23) ◽  
pp. 4685-4701 ◽  
Author(s):  
Marta M. Fay ◽  
Paul J. Anderson
Keyword(s):  

2020 ◽  
Author(s):  
Rianne Grond ◽  
Tineke Veenendaal ◽  
Juan Duran ◽  
Ishier Raote ◽  
Sebastiaan Corstjens ◽  
...  

AbstractIn vitro experiments have shown GRASP65 (GORASP1) and GRASP55 (GORASP2) proteins function in stacking Golgi cisternae. However, in vivo depletion of GORASPs in metazoans have given equivocal results. We have generated a mouse lacking both GORASPs and find that Golgi cisternae remained stacked. However, the stacks are disconnected laterally from each other and the cisternal cross-sectional diameters are significantly reduced compared to their normal counterparts. These data support earlier findings on the role of GORASPs in linking stacks and we suggest that unlinking of stacks affects dynamic control of COPI budding and vesicle fusion at the rims. The net result is that cisternal cores remain stacked, but cisternal diameter is reduced by rim consumption.


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