ArticleJournal of agricultural and food chemistry2026
Co-Refolding of Pea Protein and C-Phycocyanin for Multifunctional Hydrocolloids at pH 5.
Article in Journal of agricultural and food chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Pea proteins exhibit a low net charge near their isoelectric point (∼5), limiting their solubility and functionality. To address this limitation, we explored a pH-driven co-refolding method using C-phycocyanin, a highly hydrophilic protein that undergoes pH-dependent disassembly and reassembly. This process facilitated the formation of pea protein-C-phycocyanin hybrid hydrocolloids with enhanced stability and solubility at pH 5. The relative solubility increased from 3.9% to 68.7%, and the denaturation temperature rose from 84.2 to 129.7 °C. Structural analysis revealed the presence of large globular multimers, including at least phycocyanin nonamers complexed with legumin. Compared with C-phycocyanin alone, the hybrids enhanced the color retention of the tetrapyrrole chromophore under heat by 2.9% and under UV irradiation by 23.9%. Overall, this study demonstrates a simple and effective method to create functional plant-protein-based ingredients suitable for acidic food and beverage applications.
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