Bagchi Banerjee, Bandita, Maklad, Osama ORCID: https://orcid.org/0000-0001-6893-2654 and Acharya, Parag ORCID: https://orcid.org/0000-0003-2521-9968 (2026) Novel microparticulation of pea protein: structural transformation, enhanced gelation, dispersion stability, and off-taste masking. Food Frontiers, 7 (6):e70380. ISSN 2643-8429 (Online) (doi:10.1002/fft2.70380)

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Abstract

Pea protein isolate (PPI) suffers from poor solubility, weak gel-forming ability, and undesirable sensory attributes that limit its wider adoption in plant-based food products. This study reports a novel three-stage process for producing plant protein microparticulate by combining pH shift, high-pressure homogenization, and heat treatment. The microparticulated pea protein isolate (MPPI) demonstrated substantially improved functional properties relative to native PPI. Microparticulation reduced the volume-weighted median particle diameter (d50) approximately 10-fold (from ∼61.8 to ∼6.2 µm) and apparent particle density by ∼1.9-fold (from 1.07 to 0.57 g/cm3). The taste profiling further revealed that microparticulation altered the taste profile of PPI, with notable shifts in off-taste like astringency and bitterness. Dispersion analysis of 15% (w/w/) solution of MPPI using LUMiSizer showed an 85.5% reduction in sedimentation velocity and a 99.6% reduction in sediment height relative to PPI, reflecting markedly improved colloidal stability. Structural characterization revealed a significant reduction in surface hydrophobicity and intrinsic fluorescence intensity of MPPI compared to PPI, while free sulfhydryl content increased markedly (from 320.26 to 1571.20 nmol/mg), confirming extensive structural destabilization of MPPI due to protein unfolding and subsequent hydrophobic-core burial as well as thiol exposure. Rheological analysis demonstrated that MPPI exhibited approximately one order of magnitude higher storage modulus (G′) and consistency index (K) than native PPI, with superior structural resilience under oscillatory deformation. In situ gelation experiments showed that MPPI formed denser, mechanically stronger elastic gels upon heating and cooling, with substantially higher final G′ values. These findings therefore confirm microparticulation as an effective strategy for unlocking the structural and functional potential of PPI for wider plant-based food applications.

Item Type:	Article
Uncontrolled Keywords:	dispersion stability, high-pressure homogenization, LAOS, pea protein gelation, pea protein isolate, plant protein microparticle, plant protein
Subjects:	Q Science > Q Science (General) S Agriculture > S Agriculture (General)
Faculty / School / Research Centre / Research Group:	Faculty of Engineering & Science Faculty of Engineering & Science > Natural Resources Institute Faculty of Engineering & Science > Natural Resources Institute > Centre for Food Systems Research Faculty of Engineering & Science > School of Engineering (ENG)
Last Modified:	09 Oct 2026 13:54
URI:	https://gala.gre.ac.uk/id/eprint/54667

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