Effect of cations on the properties of high moisture textured vegetable protein: from the perspective of Hofmeister effect

High-moisture textured vegetable proteins (HMTVPs) prepared from twin-screw extrusion technology has been considered as a promising substitute for animal protein. In this study, systemic measurements were used to characterize influence of salts containing ions of Hofmeister series (KCl and CaCl 2 ) on the behavior of textural and physical properties, water distribution and migration, and microstructure formation in HMTVPs. The results showed that the added ions notably influenced the interactions between plant proteins. The addition of Ca 2+ could promote ordered arrangement and alignment of plant protein due to the directly interactions between ion and protein chains, leading a fibrous structure with enhanced texturization degree (up to 1.46). Differently, the enhanced effects in K + -contained system could only be observed at certain concentration and the characteristics present a fluctuant trend. Notably, an optimized microstructure was obtained in Ca 2+ -contained system. With this work, we provided insight into the Hofmeister series ions on physicochemical properties of HMTVPs for developing more suitable quality for future applications. • A possible mechanism based-on the Hofmeister effect to clarify the of the fibrous structural formation in HMTVPs was provided for the first time. • The microphase separation induced by water migration may be an intrinsic driving force for the formation of fiber structures. • The rheological results could be corresponding to the physicochemical properties of HMTVPs.

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Publication Details

Journal
LWT
Published
2025-06-16
DOI
https://doi.org/10.1016/j.lwt.2025.118037
Citations
5
Primary Topic
Freezing and Crystallization Processes
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article
Field-Weighted Citation Impact
4.32
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article

Effect of cations on the properties of high moisture textured vegetable protein: from the perspective of Hofmeister effect

Jingwen Ren, Yiting Guo, Xueqing Zhu, Hongzhou An et al.
5 citations
LWT
Freezing and Crystallization Processes
4.32
article

Effect of cations on the properties of high moisture textured vegetable protein: from the perspective of Hofmeister effect

Jingwen Ren, Yiting Guo, Xueqing Zhu, Hongzhou An, Yawei Zhang, Menghan Liu
article en
5 citations

Abstract

High-moisture textured vegetable proteins (HMTVPs) prepared from twin-screw extrusion technology has been considered as a promising substitute for animal protein. In this study, systemic measurements were used to characterize influence of salts containing ions of Hofmeister series (KCl and CaCl 2 ) on the behavior of textural and physical properties, water distribution and migration, and microstructure formation in HMTVPs. The results showed that the added ions notably influenced the interactions between plant proteins. The addition of Ca 2+ could promote ordered arrangement and alignment of plant protein due to the directly interactions between ion and protein chains, leading a fibrous structure with enhanced texturization degree (up to 1.46). Differently, the enhanced effects in K + -contained system could only be observed at certain concentration and the characteristics present a fluctuant trend. Notably, an optimized microstructure was obtained in Ca 2+ -contained system. With this work, we provided insight into the Hofmeister series ions on physicochemical properties of HMTVPs for developing more suitable quality for future applications. • A possible mechanism based-on the Hofmeister effect to clarify the of the fibrous structural formation in HMTVPs was provided for the first time. • The microphase separation induced by water migration may be an intrinsic driving force for the formation of fiber structures. • The rheological results could be corresponding to the physicochemical properties of HMTVPs.

LWTVol. 228
Nanjing Agricultural University (CN), Henan University of Technology (CN), National Engineering Research Center for Wheat (CN)
Zero hunger
Openalex Percentile: Top 6%
Freezing and Crystallization Processes
4.32
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