Work

Enhanced thermal stability of potato protein-pectin emulsions: Synergistic effects of bulk and interfacial properties

Year: 2026

Type: article

Abstract: Proteins and polysaccharides have been used extensively in emulsion formulation, both individually and in conjunction. However, the mechanisms underlying the thermal stability of protein-stabilized emulsions in the presence of pectin require further elucidation. Here, we systematically investigate the effect of thermal processing on such emulsions (with protein-pectin mass ratio of 1:0, 10:1, 5:1, 2:1, 1:1, and 0:1). The thermal behavior (20 ‒ 95°C) of potato protein isolate (POPI) and pectin was studied through: (1) continuous-phase properties (2) interfacial characteristics, and (3) the thermal stability of 45 wt% oil-in-water (O/W) emulsions at pH 4. POPI-pectin mixtures at ratios of 2:1 and 1:1 exhibited smaller particle size and strongly negative zeta potentials compared to higher ratios (10:1, 5:1). Heating and subsequent cooling increased both continuous-phase viscosity and interfacial elastic modulus, most probably through hydrophobic interactions, with a 2:1 ratio achieving higher interfacial elasticity values that exceed those of protein interfaces. Emulsions stabilized by the 2:1 mixture were thermally stable, maintaining small droplet sizes (∼3 μm; compared to ∼8 μm for protein-stabilized emulsions) without aggregation, coalescence, or creaming over 5 days. The enhanced thermal stability is attributed to a synergistic mechanism, in which heating induces gelation in the continuous phase and enhances elastic film formation at the interface. The findings are expected to be relevant for plant protein-stabilized emulsions, of which stability can be improved by clever combination with polysaccharides. • Potato protein and pectin jointly stabilize emulsions • Heating and subsequent cooling increases interfacial elasticity • Heating and subsequent cooling enhances bulk viscosity and storage modulus • Synergistic bulk and interfacial effects improve emulsion thermal stability

Source: LWT

DOI: 10.1016/j.lwt.2026.119050

Authors: Jiarui Cao, Meinou N. Corstens, Karin Schroën

Institution: Wageningen University & Research

Language: English

Topic: Proteins in Food Systems

Subfield: Food Science

Field: Agricultural and Biological Sciences

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $3,240

Funder: China Scholarship Council