Extraction and stability of bovine serum albumin (BSA) using cholinium-based Good's buffers ionic liquids

Abstract

Good's buffers ionic liquids (GB-ILs), composed of cholinium-based cations and Good's buffers anions, display self-buffering characteristics in the biological pH range, and their polarity and hydrophobicity can be easily tuned by a proper manipulation of their ions chemical structures. In this work, the extraction ability for bovine serum albumin (BSA) of aqueous biphasic systems (ABS) formed by polypropylene glycol 400 (PPG 400) and several GB-ILs was evaluated. ABS formed by PPG 400 and cholinium chloride ([Ch]Cl), GBs, and sucrose were also investigated for comparison purposes. It is shown that BSA preferentially migrates for the GB-IL-rich phase, with extraction efficiencies of 100%, achieved in a single-step. Dynamic light scattering, and circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopies were employed to evaluate the effect of the investigated cholinium-based GB-ILs on the BSA stability, and compared with results obtained for the respective GBs precursors, [Ch]Cl and sucrose, a well-known protein stabilizer. Molecular docking studies were also carried out to investigate on the binding sites of GB-IL ions to BSA. The experimental results confirm that BSA has a higher stability in GB-ILs than in any of the other compounds investigated.

Rapana thomasiana hemocyanin modified with ionic liquids with enhanced anti breast cancer activity

“…For example, Kumar and Venkatesu have observed that some short-chain alkyl imidazolium-based and ammonium-based ILs stabilize insulin [12,13]. High-yield extraction of proteins, antibodies and enzymes and at the same time their preserved native or active conformation in cholinium-based ionic liquid buffers have also been reported [14,15]. The effect of 1-ethyl-3-methyl-imidazolium-based ILs as refolding additives and suppressors of protein aggregation have been estimated for cardioactive peptides, lysozyme, recombinant plasminogen activators, antibody fragments, etc.…”

Controlling the l‐asparaginase extraction and purification by the appropriate selection of polymer/salt‐based aqueous biphasic systems

“…Recently, polymer/salt‐based ABS using cholinium ([Ch] + )‐based salts (or ionic liquids, ILs) were proposed as platforms for solutes partition, particularly, due to the relative hydrophobicity/hydrophilicity balance between the coexisting phases . Furthermore, it was demonstrated that [Ch] + ‐based salts can promote specific protein‐ions interactions, acting directly on the protein partitioning capacity, as shown for beta‐lactoglobulin, A and B, lysozyme, and ribonuclease A and B, as well as on protein stabilization, as previously observed for monoclonal antibodies, cytochrome c, rubisco, bovine serum albumin (BSA) and α‐chymotrypsin …”

Desenvolvimento do Processo de Produção, Isolamento e Purificação de Pigmentos produzidos por Streptomyces carpaticus

“…O pigmento a ser separado e as demais proteínas presentes no meio podem interagir através de ligações de hidrogênio, forças dispersivas ou interações eletrostáticas (Taha et al, 2015). Desta forma, considerando-se os fatores de purificação para ambos os sistemas, percebe-se que apesar do pigmento migrar majoritariamente para a fase contendo LI, não foi possível que houvesse boa separação de outras proteínas e dos demais contaminantes.…”