Ionic liquid‐based three phase partitioning (<scp>ILTPP</scp>) systems for whey protein recovery: ionic liquid selection

Alvarez‐Guerra, Enrique; Irabien, Ángel

doi:10.1002/jctb.4401

Cited by 34 publications

(32 citation statements)

References 48 publications

(101 reference statements)

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“…Alvarez‐Guerra and Irabien suggested that the salt concentration has the greatest influence on the amount of lactoferrin recovered at the interface. However, pH, temperature and protein concentration also influence the partitioning …”

Section: Resultsmentioning

confidence: 99%

“…However, pH, temperature and protein concentration also influence the partitioning. 52 The three systems studied in the current research were used previously for the partitioning of different proteins, including Rubisco. 14,29,35 No precipitation of these proteins was reported, demonstrating that the studied systems do not always form three phases.…”

Section: Protein Partitioning In Atpssmentioning

confidence: 99%

See 1 more Smart Citation

Selective and mild fractionation of microalgal proteins and pigments using aqueous two‐phase systems

Ruiz

Emmery

Wijffels

et al. 2018

J of Chemical Tech & Biotech

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BACKGROUNDMicroalgal biomass is generally used to produce a single product instead of valorizing all of the cellular components. The biomass production and downstream processes are too expensive if only one product is valorized. A new approach was proposed for the simultaneous and selective partitioning of pigments and proteins from disrupted Neochloris oleoabundans cultivated under saline and freshwater conditions.RESULTSAn aqueous two‐phase system composed of polyethylene glycol and cholinium dihydrogen phosphate selectively separated microalgal pigments from microalgal proteins. 97.3 ± 1.0% of lutein and 51.6 ± 2.3% of chlorophyll were recovered in the polymer‐rich phase. Simultaneously, up to 92.2 ± 2.0% of proteins were recovered in a third phase (interface) in between the aqueous phases (interface). The recovered proteins, including Rubisco with a molecular weight of ∼560 kDa, seem to be intact and pigments did not suffer degradation, demonstrating the mildness of this system for fractionating microalgal biomolecules.CONCLUSIONThe ability of aqueous two‐phase systems (ATPSs) to simultaneously and efficiently fractionate different biomolecules in a mild manner from disrupted microalgae is demonstrated. This is an important step towards the development of a multiproduct microalgae biorefinery. © 2018 The Authors. Journal of Chemical Technology & Biotechnology published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.

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Section: Resultsmentioning

confidence: 99%

Section: Protein Partitioning In Atpssmentioning

confidence: 99%

Selective and mild fractionation of microalgal proteins and pigments using aqueous two‐phase systems

Ruiz

Emmery

Wijffels

et al. 2018

J of Chemical Tech & Biotech

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“…The formation of an interface of precipitated proteins in these ABS could be a potential strategy to purify IgG from complex matrices within a three‐phase partitioning (TPP) approach, where the target compound is enriched at the interface of two liquid phases . The t ‐butanol and ammonium sulfate aqueous solutions are often used to induce the precipitation of biomolecules at the interface, and recently, Alvarez et al . showed that this approach is also feasible with ILs – ionic‐liquid‐based three‐phase partitioning (ILTPP).…”

Section: Resultsmentioning

confidence: 99%

Separation of immunoglobulin G using aqueous biphasic systems composed of cholinium‐based ionic liquids and poly(propylene glycol)

Ramalho

Neves

Quental

et al. 2018

J of Chemical Tech & Biotech

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Background The use of antibodies, such as immunoglobulin G (IgG), has faced a significant growth in the past decades for biomedical and research purposes. However, antibodies are high cost biopharmaceuticals, for which the development of alternative and cost-effective purification strategies is still in high demand. Results Aqueous biphasic systems (ABS) composed of poly(propylene glycol) (PPG) and cholinium-based ionic liquids (ILs) were investigated for the separation of IgG. The ABS phase diagrams were determined and characterized whenever required. Initial optimization studies with commercial IgG were carried out, followed by the extraction of IgG from rabbit serum. In all ABS, IgG preferentially partitions to the IL-rich phase, unveiling preferential interactions between IgG and ILs. Good results were obtained with commercial IgG, with extraction efficiencies ranging between 93% and 100%, and recovery yields ranging between 20% and 100%. Two of the best and two of the worst identified ABS were then evaluated in what concerns their performance to separate and recover IgG from rabbit serum. With these ABS, extraction efficiencies of 100% and recovery yields > 80% were obtained, indicating an increase in the recovery yield and extraction efficiencies when using real matrices. Under the best conditions studied, IgG with a purity level of 49% was obtained in a single-step. This purity level of IgG is higher than those previously reported using other IL-polymer ABS. Conclusion IgG preferentially migrates to the IL-rich phase in ABS formed by ILs and polymers, allowing the design of effective separation systems for its recovery from serum samples.

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“…Hence, in this section, we have tried together all these research reports under the same roof, so that it is easily available to the readers and also to expose its importance to the scientific world. An overview of the literature reveals stability studies of proteins such as amyloglucosidase [79], thyroglobulin [79], glutamate dehydrogenase [79], lactate dehydrogenase [79], glucose dehydrogenase [80], formate dehydrogenase [94], glycosidase (α and β) [81], monellin [82], β-galactosidase [83], glucose oxidase [106], lactate oxidase [109], oxidoreductases [107], subtilisin Carlsberg [84], Amano protease P6 [85], pepsin [86], papain [87,100] esterases from Bacillus subtilis and Bacillus stearothermophilus [87], Penicillium expansum lipase [88], mushroom tyrosinase [88], chloroperoxidase [89], porcine pancreatic lipase [91], α-helical protein Im7 [92], pepsin [93], adenosine deaminase [95], α-amylases [96], xylanase II (GH11 enzyme, from Trichoderma longibrachiatum [97], lactoferrin [99], α-synuclein [101,103], ribonuclease A [102], casein [104,105], epoxide hydrolase [110], avidin [111], Abeta peptide [112], zein [113] and firefly luciferase (Photinus pyralis luciferase) in the ILs. Among them some of the proteins have been stabilized [79]…”

Section: Structure and Stability Of Some Other Proteins In Different Ilsmentioning

confidence: 99%

The Role of Ionic Liquids in Protein Folding/Unfolding Studies

Kumar¹,

Bisht²,

Jha³

et al. 2017

Progress and Developments in Ionic Liquids

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Ionic liquids (ILs) have emerged as novel solvent medium for several biotechnological processes in vitro. The use of ILs starts from protein extraction to catalysis to folding/ unfolding studies. ILs are becoming the most favorite non-aqueous medium for protein studies due to their unique ionic combinations (cation + anion) and tunable physical properties. In this context, several research results have been published that use of pure or aqueous IL solutions as stabilizer for proteins. Hence, herein, in this chapter, we present a collection of research work that focuses on the importance of ILs (and their mixture) in protein stabilities. In addition, we have also reviewed the unique properties of ILs as counteracting solvents for cold-induced denaturation and also their refolding properties. This report will definitely generate a new understanding for the ILs, their importance and applicability in protein folding studies.that is now considered as the first IL is ethylammonium nitrate ([C 2 H 5 NH 3 ][NO 3 ], EAN) and was prepared by Paul Walden in 1914 and has a melting point of 12°C [8]. After a long gap, the major studies of room temperature molten salts of pyridinium halides with aluminum chloride (AlCl 3 ) were made in the 1940s by a group led by Frank Hurley and Tom Weir at Rice University [9]. Later, alkylimidazolium salts (C n mim) + were also reported in the early 1980s [10]. An excellent short history of the birth of ILs, which covers the crucial moments of this area, is presented by John S. Wilkes [11].In its initial revolutionary stage, ILs were vastly considered in analytical chemistry based on their unique and tunable physical properties. Since then, synthesis of a large number of multifunctional ILs has been a prime interest for synthetic chemists [12,13]. In this context, varieties of task-specific ILs have been synthesized and the advantages of their physical properties have been reported in an open literature [14]. Common ILs include ammonium, phosphonium, sulfonium, guanidinium, pyridinium, imidazolium and pyrrolidinium cations. The most common anions are chloride, bromide, tetrafluoroborate, hexafluorophosphate, trifluoromethanesulfonyl, bis(trifluoromethanesulfonyl)imide, dicyanamide and alkyl sulfate anions. These ILs have some unique properties such as negligible vapor pressure, good thermal stability, tunable viscosity and miscibility with water, a wide electrochemical window, high conductivity and high heat capacity [15][16][17]. These physical properties make IL a promising material in numerous fields, for example, their use in electrochemical devices and replacements for several organic reactions [18,19]. Gordon [20], Parvulescu and Hardacre [21] and Crowhurst et al. [22] pointed out that there is an obvious advantage in performing many reactions in ILs due to the improvement in reaction activity, selectivity and yield. An in-depth literature survey reveals that there tremendously exist a large number of scholarly articles as well as elegant reviews that explicitly elucidate the various s...

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Ionic liquid‐based three phase partitioning (ILTPP) systems for whey protein recovery: ionic liquid selection

Cited by 34 publications

References 48 publications

Selective and mild fractionation of microalgal proteins and pigments using aqueous two‐phase systems

Selective and mild fractionation of microalgal proteins and pigments using aqueous two‐phase systems

Separation of immunoglobulin G using aqueous biphasic systems composed of cholinium‐based ionic liquids and poly(propylene glycol)

The Role of Ionic Liquids in Protein Folding/Unfolding Studies

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