ArticleFoods (Basel, Switzerland)2023
Ionic Strength Dependence of the Complex Coacervation between Lactoferrin and β-Lactoglobulin.
Article in Foods (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Probiotic microcapsule polysaccharide-protein composite system: construction, mechanism and application.Archives of microbiology · 2026Review
- Anomalous Liquid-Liquid Phase Separation Dynamics in Polymerization-Driven Complex Coacervation.ACS macro letters · 2026Article
- Chitosan nanoparticles for mucosal and needle-free vaccination.NPJ vaccines · 2026Review
- Article
- Biomolecule-Based Coacervation: Mechanisms, Applications, and Future Perspectives in Biomedical and Biotechnological Fields.Biomolecules · 2025Review
- Preparation of Polymyxin B-Functionalized Cryogels for Efficient Endotoxin Removal from Protein Solutions.Gels (Basel, Switzerland) · 2025Article
- pH-Dependent Extraction of Antioxidant Peptides from Red SeaweedMarine drugs · 2024Article
- The Multifaceted Roles of Bovine Lactoferrin: Molecular Structure, Isolation Methods, Analytical Characteristics, and Biological Properties.Journal of agricultural and food chemistry · 2023Review
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Authors and funding
5 authors.
Funding
Abstract
Heteroprotein complex coacervation is an assembly formed by oppositely charged proteins in aqueous solution that leads to liquid-liquid phase separation. The ability of lactoferrin and β-lactoglobulin to form complex coacervates at pH 5.5 under optimal protein stoichiometry has been studied in a previous work. The goal of the current study is to determine the influence of ionic strength on the complex coacervation between these two proteins using direct mixing and desalting protocols. The initial interaction between lactoferrin and β-lactoglobulin and subsequent coacervation process were highly sensitive to the ionic strength. No microscopic phase separation was observed beyond a salt concentration of 20 mM. The coacervate yield decreased drastically with increasing added NaCl from 0 to 60 mM. The charge-screening effect induced by increasing the ionic strength is attributed to a decrease of interaction between the two oppositely charged proteins throughout a decrease in Debye length. Interestingly, as shown by isothermal titration calorimetry, a small concentration of NaCl around 2.5 mM promoted the binding energy between the two proteins. These results shed new light on the electrostatically driven mechanism governing the complex coacervation in heteroprotein systems.
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