Abstract
In this work, the extraction and separation of bovine serum albumin (BSA) from its original matrix, i.e., bovine serum, was performed using a novel ionic-liquid-based aqueous biphasic system (IL-based ABS). To this end, imidazolium-, phosphonium-, and ammonium-based ILs, combined with the anions’ acetate, arginate and derived from Good Buffers, were synthesized, characterized, and applied in the development of ABS with K2HPO4/KH2PO4 buffer aqueous solutions at pH 7. Initial studies with commercial BSA revealed a preferential migration of the protein to the IL-rich phase, with extraction efficiencies of 100% obtained in a single-step. BSA recovery yields ranging between 64.0% and 84.9% were achieved, with the system comprising the IL tetrabutylammonium acetate leading to the maximum recovery yield. With this IL, BSA was directly extracted and separated from bovine serum using the respective ABS. Different serum dilutions were further investigated to improve the separation performance. Under the best identified conditions, BSA can be extracted from bovine serum with a recovery yield of 85.6% and a purity of 61.2%. Moreover, it is shown that the BSA secondary structure is maintained in the extraction process, i.e., after being extracted to the IL-rich phase. Overall, the new ABS herein proposed may be used as an alternative platform for the purification of BSA from serum samples and can be applied to other added-value proteins.
Highlights
The extraction efficiency pure bovine serum albumin (BSA), a protein profile with a rich α-helix structure is presented, with two minimums and yield of pure BSA were evaluated for each system under study
Overall, is this herework shown composed of properly obtaineditin forthat aqueous solutionsdesigned are very quaternary similar for the α-helix ammonium-based Ionic liquids (ILs) should be more deeply investigated in the field of proteins separation since they provide a biocompatible environment and present a lower cost when compared with the widely studied imidazolium-based counterparts
The aim of this work was the development of novel IL-based Aqueous biphasic systems (ABS) as appropriate protein separation platforms and to provide a better understanding of the conditions required to apply these ABS without leading to the protein’s loss of stability
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. Proteins play a fundamental role in biological processes and have high value in different industrial applications, e.g., in the food, biopharmaceutical or cosmetic industries [1]. Conventional techniques for proteins separation and purification include chromatography, electrophoresis, precipitation, and filtration-related techniques, among others [2]. There is a need of finding more cost-effective techniques to efficiently separate and purify proteins, while being capable of maintaining their native structure and function/activity [3]
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