Improving the Gelation Properties of Pea Protein Isolates Using Psyllium Husk Powder: Insight into the Underlying Mechanism

• Published in: Foods 2024-10, Vol.13 (21), p.3413
• Main Authors: Chen, Qiongling, Guan, Jiewen, Wang, Zhengli, Wang, Yu, Wang, Xiaowen, Chen, Zhenjia
• Format: Article
• Language: English
• Subjects: Amino groups; Cellulose; conformational change; Dietary fiber; Electrostatic properties; Food; Food plants; Fourier analysis; Fourier transforms; Gelation; gelation mechanism; Gels; Hydrogen; Hydrogen bonding; Hydrophobicity; Industrial applications; Infrared analysis; Infrared spectroscopy; Intermolecular forces; Molecular interactions; Nanocrystals; pea protein; Peas; protein gel; Proteins; Psyllium; psyllium husk powder; Rheological properties; Rheology; Scanning electron microscopy; Surface active agents; Vegetable industry; Viscoelasticity
• ISSN: 2304-8158; 2304-8158
• DOI: 10.3390/foods13213413

The industrial application of pea protein is limited due to its poor gelation properties. This study aimed to evaluate the effects of psyllium husk powder (PHP) on improving the rheological, textural, and structural properties of heat-induced pea protein isolate (PPI) gel. Scanning electron microscopy (SEM), intermolecular forces analysis, the quantification of the surface hydrophobicity and free amino groups, and Fourier transform infrared spectroscopy (FTIR) were conducted to reveal the inner structures of PPI-PHP composite gels, conformational changes, and molecular interactions during gelation, thereby clarifying the underlying mechanism. The results showed that moderate levels of PHP (0.5-2.0%) improved the textural properties, water holding capacity (WHC), whiteness, and viscoelasticity of PPI gel in a dose-dependent manner, with the WHC (92.60 ± 1.01%) and hardness (1.19 ± 0.02 N) peaking at 2.0%. PHP significantly increased surface hydrophobicity and enhanced hydrophobic interactions, hydrogen bonding, and electrostatic interactions in PPI-PHP composite gels. Moreover, the electrostatic repulsion between anionic PHP and negatively charged PPI in a neutral environment prevented the rapid and random aggregation of proteins, thereby promoting the formation of a well-organized gel network with more β-sheet structures. However, the self-aggregation of excessive PHP (3.0%) weakened molecular interactions and disrupted the continuity of protein networks, slightly reducing the gel strength. Overall, PHP emerged as an effective natural gel enhancer for the production of pea protein gel products. This study provides technical support for the development of innovative plant protein-based foods with strong gel properties and enriched dietary fiber content.