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Updated: Mar 9, 2026

Study of Short Peptide Adsorption on Solution Dispersed Inorganic Nanoparticles Using Depletion Method
Published on: April 11, 2020
Insoluble and soluble pea proteins at air-water and oil-water systems: Adsorption and interfacial network formation
Sung Yoon Lim1, Galo Chuchuca Moran1, Lutz Grossmann1
1Department of Food Science, University of Massachusetts Amherst, 100 Holdsworth Way, Amherst, MA 01003, USA.
Abstract:
Pea proteins are a common plant protein source that consists of an insoluble (globulin-rich) and soluble (albumin-rich) fraction with potentially synergistic interfacial properties. The aim of this study was to systematically examine the interfacial rheology and interfacial tension of PPI and SPP, both as individual fractions and in combination, to identify their complementary functional roles. The soluble pea protein fraction exhibited high solubility, low surface hydrophobicity, and a high content of albumins in the small molecular weight range (<25 kDa in ∼75% of the total proteins). Conversely, insoluble pea protein fraction showed lower solubility, high surface hydrophobicity, and a high variety of large proteins, mostly globulins (>30 kDa in ∼76% of the total proteins). Individually, the soluble fraction exhibited a slower reduction in surface and interfacial tension, but faster and stronger viscoelastic network development at the air-water surface with overall higher moduli (Gi' = 19.5 ± 4.0 vs. 34.4 ± 6.0 mPa m). When combined, no synergistic effects were observed in viscoelastic interfacial/surface network formation, indicating that blending the fractions mainly compensated for individual limitations without surpassing the performance of the individual fractions. In contrast, the mixtures exhibited clear synergy in interfacial energy, with formulations rich in the soluble fraction reducing surface tension by up to 12% and interfacial tension by up to 46% compared to the individual fractions.
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