scholarly journals Phase separation dynamics of gluten protein mixtures

Soft Matter ◽  
2019 ◽  
Vol 15 (30) ◽  
pp. 6160-6170 ◽  
Author(s):  
Amélie Banc ◽  
Justine Pincemaille ◽  
Salvatore Costanzo ◽  
Edouard Chauveau ◽  
Marie-Sousai Appavou ◽  
...  

We investigate by time-resolved synchrotron ultra-small X-ray scattering the dynamics of liquid–liquid phase-separation of gluten protein suspensions following a temperature quench and show that viscous and gel samples exhibit distinctive features.

2020 ◽  
Vol 4 (10) ◽  
pp. 1888-1894
Author(s):  
Chris J. Benmore ◽  
Oliver L. G. Alderman ◽  
Sophie R. Benmore ◽  
Stephen K. Wilke ◽  
Richard J. K. Weber

2013 ◽  
Vol 1518 ◽  
pp. 47-52
Author(s):  
S.V. Stefanovsky ◽  
B.S. Nikonov ◽  
B.I. Omelyanenko ◽  
K.M. Fox ◽  
J.C. Marra

ABSTRACTGlasses in the Al2O3-B2O3-Fe2O3-Na2O-SiO2 system were produced at a temperature of 1150 °C, annealed, and examined using XRD and SEM/EDX. Surfaces of same samples were additionally heat-treated and etched with HCl. The pristine samples were X-ray amorphous and rather homogeneous except the B1 sample that contained trace crystalline phases of carnegieite/nepheline and spinel. Corrosion of these glasses via an etching treatment proceeds by a conventional mechanism with damage of their surface layers, however, the B2 glass exhibits a “drop-type” microstructure after etching that suggests occurrence of liquid-liquid phase separation.


2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Erik W. Martin ◽  
Tyler S. Harmon ◽  
Jesse B. Hopkins ◽  
Srinivas Chakravarthy ◽  
J. Jeremías Incicco ◽  
...  

AbstractCompartmentalization by liquid-liquid phase separation (LLPS) has emerged as a ubiquitous mechanism underlying the organization of biomolecules in space and time. Here, we combine rapid-mixing time-resolved small-angle X-ray scattering (SAXS) approaches to characterize the assembly kinetics of a prototypical prion-like domain with equilibrium techniques that characterize its phase boundaries and the size distribution of clusters prior to phase separation. We find two kinetic regimes on the micro- to millisecond timescale that are distinguished by the size distribution of clusters. At the nanoscale, small complexes are formed with low affinity. After initial unfavorable complex assembly, additional monomers are added with higher affinity. At the mesoscale, assembly resembles classical homogeneous nucleation. Careful multi-pronged characterization is required for the understanding of condensate assembly mechanisms and will promote understanding of how the kinetics of biological phase separation is encoded in biomolecules.


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