Accumulation of small protein molecules in a macroscopic complex coacervate. Issue 2 (19th October 2015)

• Record Type: Journal Article
• Authors: Lindhoud, Saskia; Claessens, Mireille M. A. E.
• Is Part Of: Soft matter. Volume 12:Issue 2(2016)
• Page Start: 408
• Page End: 413
• Publication Date: 2015-10-19
• Subjects: Soft condensed matter -- Periodicals; 530.413
• DOI: 10.1039/c5sm02386f
• Languages: English
• ISSNs: 1744-683X

Abstract

Abstract : By mixing the aqueous solutions of poly acrylic acid, poly-( N, N dimethylaminoethyl methacrylate) and lysozyme, complex coacervates with a protein concentration as high as 200 g L −1 are obtained. Abstract : To obtain insight into the accumulation of proteins into macroscopic complex coacervate phases, the lysozyme concentration in complex coacervates containing the cationic polyelectrolyte poly-( N, N dimethylaminoethyl methacrylate) and the anionic polyelectrolyte polyacrylic acid was investigated as a function of the mixing ratio, protein concentration and ionic strength. Maximal protein enrichment of the complex coacervate phase was observed to require the presence of all three macromolecules. Under optimized conditions the protein concentrations in the complex coacervate were as high as 200 g L −1 . Such high concentrations are comparable to the protein concentration in the cytosol, suggesting that these interesting liquid phases may serve a suitable model system for the phase behavior of the cytosol and genesis and function of membrane-less organelles. The high stability of the complexes and the salt dependent uptake of protein suggest that complex coacervates may provide a way to store hydrated proteins at high concentrations and might therefore be of interest in the formulation of high protein foods.