Synergistic effect of hydrophilic polyglycerol fatty acid esters and protein on the stability of interfacial membrane in low-fat aerated emulsions with different homogenization conditions

Han W 1 , Chai X 1 , Zaaboul F 2 , Sun Y 1 , Tan CP 3 , Liu Y 4

Affiliations 

  • 1 State Key Laboratory of Food Science and Technology, School of Food Science and Technology, National Engineering Research Center for Functional Food, National Engineering Laboratory for Cereal Fermentation Technology, Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Jiangnan University, 1800 Lihu Road, Wuxi 214122, Jiangsu, People's Republic of China
  • 2 Food and Biomaterials Group, School of Biosciences, University of Nottingham, LE12 5RD, United Kingdom
  • 3 Department of Food Technology, Faculty of Food Science and Technology, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia
  • 4 State Key Laboratory of Food Science and Technology, School of Food Science and Technology, National Engineering Research Center for Functional Food, National Engineering Laboratory for Cereal Fermentation Technology, Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Jiangnan University, 1800 Lihu Road, Wuxi 214122, Jiangsu, People's Republic of China. Electronic address: yfliu@jiangnan.edu.cn
Food Chem, 2024 Mar 01;435:137584.
PMID: 37774617 DOI: 10.1016/j.foodchem.2023.137584

Abstract

This study investigates the impact of various chain lengths of hydrophilic polyglycerol fatty acid esters (HPGEs), namely SWA-10D, M-7D and M-10D on protein interactions and their influence on the surface morphology and interfacial properties of low-fat aerated emulsions under different pressures conditions. M-7D and M-10D samples exhibited larger particle sizes, higher ζ-potential and rougher surface compared to SWA-10D sample at 1 % concentration of HPGEs. Consequently, M-7D and M-10D samples demonstrated lower values of G', G'', and higher values tan δ at the oil-water interface as pressure increased, thereby promoting the formation of less viscoelastic structures. M-7D sample, characterized by lower content of α-helix structures, resulted in an observable redshift in the NH and CO groups of the protein. Molecular docking analysis affirmed that M-7D sample exhibited a lower absolute binding energy value, indicating stronger interaction with the protein compared to other samples, ultimately contributing to the unstable interfacial membrane formed.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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