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Role of gellan gum in multiscale assembly and structure-property relationships of potato protein-soybean protein fibril-pea protein fibril composite gels

Journal 2026 · IF 8.7 · 发表于 2026 年 9 月 29 日
作者: Jing-Wen Zhang,Hui-Lin Li,Qin Yang,Qing-Xuan Liu,Han-Qing Chen
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摘要

2.0 wt% gellan gum minimized apparent porosity (50.55%) and apparent D50 (4.61 μm). • Gel strength and WHC showed non-monotonic responses, peaking at 3.0 wt%. • Thermo-mechanical metrics correlated with -SH, hydrogen bonds, Tp-heating and k'. • Pore structure reflected hydrophobicity, nonspecific binding and viscoelasticity. • Residual Mantel revealed links beyond concentration co-variation. Multicomponent gels integrating globular plant proteins with protein fibrils offer a promising soft-matter route for texture design in plant-based meat analogues (PBMAs), yet the polysaccharide-mediated multiscale assembly underlying their structure–property relationships remains poorly understood. In this study, gellan gum (0–4.0 wt%) was used to modulate composite gels comprising potato protein, soybean protein fibrils, and pea protein fibrils (2:1:1, w /w/w). Gellan gum modulated the pre-assembly state, as indicated by changes in apparent soluble-protein fraction, ζ-potential, ANS-derived surface hydrophobicity, and DTNB-reactive -SH content, while gel strength and water holding capacity showed concentration-dependent responses among the self-supporting formulations, with the highest mean values observed at 3.0 wt% gellan gum. Quantitative SEM (500×) revealed concurrent pore refinement, reaching the lowest apparent porosity (50.55%) and apparent D50 (4.61 μm) at 2.0 wt% gellan gum, whereas 4.0 wt% gellan gum partially reintroduced larger pores (apparent D50, 5.71 μm). A concentration-adjusted Mantel analysis was used to separate concentration-driven co-variation from robust links between interactions, thermo-rheology and pore architecture. These results reveal a concentration-dependent trade-off between pore refinement, structural uniformity, and mechanical rigidity, offering a mechanistic basis for soft-matter structuring of PBMAs. Download: Download high-res image (207KB) Download: Download full-size image