Intermolecular interactions during complex coacervation of pea protein isolate and gum arabic

Journal of Agricultural and Food Chemistry
Shuanghui LiuMichael T Nickerson

Abstract

The nature of intermolecular interactions during complexation between pea protein isolate (PPI) and gum arabic (GA) was investigated as a function of pH (4.30-2.40) by turbidimetric analysis and confocal scanning microscopy in the presence of destabilizing agents (100 mM NaCl or 100 mM urea) and at different temperatures (6-60 degrees C). Complex formation followed two pH-dependent structure-forming events associated with the formation of soluble and insoluble complexes and involved interactions between GA and PPI aggregates. Complex formation was driven by electrostatic attractive forces between complementary charged biopolymers, with secondary stabilization by hydrogen bonding. Hydrophobic interactions were found to enhance complex stability at lower pH (pH 3.10), but not with its formation.

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Citations

Dec 3, 2013·International Journal of Pharmaceutics·Emil Meng-LundJette Jacobsen
Aug 8, 2012·Food Chemistry·Guo-Qing HuangJian Yang
Jun 29, 2018·Journal of the Science of Food and Agriculture·Sumudu N Warnakulasuriya, Michael T Nickerson
May 9, 2019·Journal of Food Science·Ruth Hernández-NavaMaría Teresa Jiménez-Munguía
Apr 10, 2021·International Journal of Biological Macromolecules·Fotini PlatiAdamantini Paraskevopoulou
Jun 10, 2015·International Journal of Biological Macromolecules·Mohammad AnvariDonghwa Chung
Jul 31, 2021·ACS Applied Materials & Interfaces·Xiufeng LiRenko de Vries
Mar 30, 2011·The Journal of Physical Chemistry. B·Ebru KizilayPaul L Dubin
Jul 8, 2014·Journal of Agricultural and Food Chemistry·Xingfei LiCaimeng Zhang
Oct 21, 2021·Journal of Agricultural and Food Chemistry·Demei MengRui Yang
Nov 16, 2018·International Journal of Biological Macromolecules·Jun-Xia XiaoGuo-Qing Huang

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