English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Resolving the mechanisms of soy glycinin self-coacervation and hollow-condensate formation

Chen, N., Zhao, Z., Wang, Y., & Dimova, R. (2020). Resolving the mechanisms of soy glycinin self-coacervation and hollow-condensate formation. ACS Macro Letters, 9(12), 1844-1852. doi:10.1021/acsmacrolett.0c00709.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files
hide Files
:
Article.pdf (Publisher version), 6MB
Name:
Article.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-

Locators

show

Creators

show
hide
 Creators:
Chen, Nannan1, Author              
Zhao, Ziliang1, Author              
Wang, Yong, Author
Dimova, Rumiana1, Author              
Affiliations:
1Rumiana Dimova, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863328              

Content

show
hide
Free keywords: Salts, Peptides and proteins, Molecular mechanics, Hollow structures, Phase transitions
 Abstract: Self-coacervation of animal-derived proteins has been extensively investigated while that of plant proteins remains largely unexplored. Here, we study the process of soy glycinin self-coacervation and transformation into hollow condensates. The protein hexameric structure composed of hydrophilic and hydrophobic polypeptides is crucial for coacervation. The process is driven by charge screening of the intrinsically disordered region of acidic polypeptides, allowing for weak hydrophobic interactions between exposed hydrophobic polypeptides. We find that the coacervate surface exhibits order, which stabilizes the coacervate shape during hollow-condensate formation. The latter process occurs via nucleation and growth of protein-poor phase in the coacervate interior, during which another ordered layer at the inner surface is formed. Aging enhances the stability of both coacervates and hollow condensates. Understanding plant protein coacervation holds promises for fabricating novel functional materials.

Details

show
hide
Language(s): eng - English
 Dates: 2020-12-062020
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1021/acsmacrolett.0c00709
BibTex Citekey: doi:10.1021/acsmacrolett.0c00709
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: ACS Macro Letters
  Abbreviation : ACS Macro Lett.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 9 (12) Sequence Number: - Start / End Page: 1844 - 1852 Identifier: ISSN: 2161-1653