A combined approach for modifying pea protein isolate to greatly improve its solubility and emulsifying stability

Zijian Zhi; Lei Yan; Hao Li; Koen Dewettinck; Paul Van der Meeren; Rui Liu; Filip Van Bockstaele

doi:10.1016/j.foodchem.2021.131832

A combined approach for modifying pea protein isolate to greatly improve its solubility and emulsifying stability

Food Chem. 2022 Jun 30:380:131832. doi: 10.1016/j.foodchem.2021.131832. Epub 2021 Dec 17.

Authors

Zijian Zhi¹, Lei Yan², Hao Li³, Koen Dewettinck⁴, Paul Van der Meeren³, Rui Liu⁵, Filip Van Bockstaele⁴

Affiliations

¹ Food Structure and Function (FSF) Research Group, Department of Food Technology, Safety and Health, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, 9000 Gent, Belgium. Electronic address: zijian.zhi@ugent.be.
² State Key Laboratory of Food Nutrition and Safety, Tianjin University of Science & Technology, Tianjin 300457, China.
³ Particle and Interfacial Technology Group (PaInT), Department of Green Chemistry and Technology, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, 9000 Gent, Belgium.
⁴ Food Structure and Function (FSF) Research Group, Department of Food Technology, Safety and Health, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, 9000 Gent, Belgium.
⁵ Food Structure and Function (FSF) Research Group, Department of Food Technology, Safety and Health, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, 9000 Gent, Belgium; State Key Laboratory of Food Nutrition and Safety, Tianjin University of Science & Technology, Tianjin 300457, China. Electronic address: lr@tust.edu.cn.

PMID: 35144133
DOI: 10.1016/j.foodchem.2021.131832

Abstract

Pea protein-based delivery systems have drawn much attention in the food and pharmaceutical fields in recent years. However, its broad application faces great limitations because of the low solubility. Here, we present a novel and effective approach to overcome this difficulty and enhance the techno-functional characteristics, especially emulsifying stability, of the pea protein isolate (PPI). By combining pH-shifting with ultrasound and heating (PUH), we concluded that the solubility of PPI greatly increased from 29.5 % to 90.4 %, whereas its surface hydrophobicity increased from 1098 to 3706. This was accompanied by the changes of PPI structure, as shown by circular dichroism and scanning electron microscopy. In addition, the modified PPI was applied to stabilize sunflower oil-in-water emulsions. The droplet size of the emulsion with PUHP was reduced and its emulsion stability was significantly elevated. Taken together, we propose a novel combined approach to prepare modified PPI with high solubility and emulsion stability. We expect our method will have a wider application in modifying plant proteins and improving their industrial processing.

Keywords: Emulsion stability; Heating; PH-shifting; Pea protein isolate; Solubility; Ultrasound.

MeSH terms

Emulsifying Agents
Emulsions
Hydrophobic and Hydrophilic Interactions
Pea Proteins*
Solubility

Substances

Emulsifying Agents
Emulsions
Pea Proteins