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Updated: Jul 5, 2026

Isolation and Characterization of Intact Phycobilisome in Cyanobacteria
Published on: November 10, 2021
Aggregate status determining the foaming behavior of phycocyanin: insights from bulk phase and air-water interface
Qingxuan Fu1, Jingjing Wang2, Fangcheng Jiang3
1Key Laboratory for Deep Processing of Major Grain and Oil, School of Food Science and Engineering, Wuhan Polytechnic University, Wuhan, Hubei 430023, PR China.
Abstract:
C-phycocyanin (C-PC) exhibits diverse foaming properties under acidic pH conditions (5.6-2.0), but the relationship between pH-induced structural changes and air-water interfacial properties is unclear. At pH 5.6 and 5.0, C-PC proteins remained segregated, forming a relatively denser interfacial layer with typical strain hardening during the compression of the interface. At pH 4.0 and 3.0, C-PC proteins formed large aggregates (100-500 nm) and exhibited Pickering-like characteristics. As surface hydrophobicity increased, the foaming capacity increased to ∼100%. At pH 2.0, a mixture of segregated proteins and smaller aggregates (30-50 nm) showed the highest adsorption rate and the highest interfacial modulus, which resulted in a foaming capacity of 147%. This study theoretically understands the pH-induced changes in protein structure and aggregate states, and illustrates how these changes result in the excellent foaming properties. It also expands the application of C-PC as a functional alternative protein in high-efficiency foaming agents.
