Soy protein particles with enhanced anti-aggregation behaviors under various heating temperatures, pH, and ionic strengths

Xiaohan Zheng; Chao Ren; Yixue Wei; Jiamei Wang; Xianbing Xu; Ming Du; Chao Wu

doi:10.1016/j.foodres.2023.112924

Soy protein particles with enhanced anti-aggregation behaviors under various heating temperatures, pH, and ionic strengths

Food Res Int. 2023 Aug:170:112924. doi: 10.1016/j.foodres.2023.112924. Epub 2023 May 2.

Authors

Xiaohan Zheng¹, Chao Ren¹, Yixue Wei¹, Jiamei Wang¹, Xianbing Xu¹, Ming Du¹, Chao Wu²

Affiliations

¹ School of Food Science and Technology, Dalian Polytechnic University, Dalian, 116034, China; National Engineering Research Center of Seafood, China; Liaoning Key Laboratory of Food Nutrition and Health, China; Collaborative Innovation Center of Provincial and Ministerial Co-construction for Seafood Deep Processing, China.
² School of Food Science and Technology, Dalian Polytechnic University, Dalian, 116034, China; National Engineering Research Center of Seafood, China; Liaoning Key Laboratory of Food Nutrition and Health, China; Collaborative Innovation Center of Provincial and Ministerial Co-construction for Seafood Deep Processing, China. Electronic address: wuchao@dlpu.edu.cn.

PMID: 37316041
DOI: 10.1016/j.foodres.2023.112924

Abstract

Protein-containing food products are frequently heated during processing to passivate anti-nutritional components. However, heating also contributes to protein aggregation and gelation, which limits its application in protein-based aqueous systems. In this study, heat-stable soy protein particles (SPPs) were fabricated by preheating at 120 °C for 30 min and at 0.5% (w/v) protein concentration. Compared to untreated soy proteins (SPs), SPPs exhibited a higher denaturation ratio, stronger conformational rigidity, compacter colloidal structure, and higher surface charge. The aggregation state of SPs and SPPs at various heating conditions (temperatures, pH, ionic strength, and types) was analyzed by dynamic light scattering, atomic force microscopy, and cryo-scanning electron microscopy. SPPs showed less increase in particle size and greater anti-aggregation ability than SPs. When heated in the presence of salt ions (Na⁺, Ca²⁺) or at acidic conditions, both SPs and SPPs formed larger spherical particles, but the size increase rate of SPPs was significantly lower than SPs. These findings provide theoretical information for preparing heat-stable SPPs. Furthermore, the development of SPPs is conducive to designing protein-enriched ingredients for producing innovative foods.

Keywords: Anti-aggregation behavior; Conformational feature, different conditions; Heat stability; Soy proteins.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Heating*
Hydrogen-Ion Concentration
Osmolar Concentration
Soybean Proteins*
Temperature

Substances

Soybean Proteins