The influence of salts on the phase composition in aqueous two-phase systems: experiments and predictions

Salabat, Alireza

doi:10.1016/s0378-3812(01)00569-6

Cited by 46 publications

(34 citation statements)

References 17 publications

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“…So, more salting-out effect causes more recovery of zein in the top phase and more recovery of BSA and ȕ-LG in the bottom phase of PPG + salts + H 2 O systems. The recovery results in Table 3 show that this trend is as Na 2 SO 4 > MgSO 4 > (NH 4 ) 2 SO 4 , which agrees with the saltingout power of these salts in the PPG + salts + H 2 O systems [20]. Figure 1 shows the gel electrophoresis of BSA in top and bottom phases of the PPG + MgSO 4 + H 2 O system, as a typical system.…”

Section: Effect Of Nature Of Saltsupporting

confidence: 71%

“…Our previous liquid-liquid equilibrium data for aqueous PPG/salts and PEG/salt systems [19][20] were used for the preparation of two-phase samples; so the salt and polymer concentration were known for all tie-lines. The protein concentrations were determined by dye binding method, using Coomassie brilliant blue G250 [22] for BSA and ȕ-LG.…”

Section: Analysis Of Samplesmentioning

confidence: 99%

“…used in this work. These systems have been studied previously in detail [19][20]. The tie line length (TLL) was calculated by the following equation: …”

Section: Gel Electrophoresis Analysismentioning

confidence: 99%

“…In our previous research works liquid-liquid phase diagrams of PPG425/salts (MgSO 4 , (NH 4 ) 2 SO 4 , Na 2 SO 4 )/ water [19], and PEG6000/MgSO 4 /water [20] systems were investigated. Partitioning of some amino acids was also investigated in aqueous two-phase system of PPG425 + MgSO 4 + H 2 O [21].…”

Section: Introductionmentioning

confidence: 99%

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Application of aqueous mixtures of polypropylene glycol or polyethylene glycol with salts in proteomic analysis

Salabat

Abnousi

Motahari

2010

JICS

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Partitioning of Bovine serum albumin (BSA), ȕ-lactoglobulin (ȕ-LG) and zein as model proteins in aqueous two-phase systems (S) containing polypropylene glycol (PPG425) or polyethylene glycol (PEG 6000) and salts (MgSO 4 , (NH 4 ) 2 SO 4 , Na 2 SO 4 ) is presented in this paper. The effects of different factors such as tie-line length, salt type and polymer type on the partition coefficient and recovery percent of proteins were analysed. The model proteins were separated by these systems (S) and directly used for gel electrophoresis without separating the target proteins from phase-forming reagents. The results revealed that the S, studied in this work could be used as a novel prefractionation method in proteomic analysis and could separate proteomic proteins in multigroup by one step extraction.

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Section: Effect Of Nature Of Saltsupporting

confidence: 71%

Section: Analysis Of Samplesmentioning

confidence: 99%

“…used in this work. These systems have been studied previously in detail [19][20]. The tie line length (TLL) was calculated by the following equation: …”

Section: Gel Electrophoresis Analysismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Application of aqueous mixtures of polypropylene glycol or polyethylene glycol with salts in proteomic analysis

Salabat

Abnousi

Motahari

2010

JICS

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“…Salabat (2001) demonstrated the influence of different salts on the phase composition in aqueous two phase systems. Klomklao et al (2005) studied the effect of different salts on the partition behavior of proteinases from tuna spleen in ATPS and observed that ATPS system consisting of PEG 1000 and magnesium sulphate provided the best condition for maximum partitioning of proteinases in PEG rich top phase.…”

Section: Resultsmentioning

confidence: 99%

Purification of alkaline protease from chicken intestine by aqueous two phase system of polyethylene glycol and sodium citrate

et al. 2010

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An aqueous two phase system of polyethylene glycol (PEG) and salts was evaluated for separation and purification of alkaline proteases from chicken intestine. Among the different salts evaluated potassium phosphate and sodium citrate gave higher enzyme yield (73.5% and 69.7% respectively) and enzyme purification (5.3 and 7.4 fold) in PEG rich upper phase. Increase in concentration of sodium citrate in the system resulted in reduction in enzyme yield and enzyme purification factor, with 15% salt showing highest enzyme yield (59.8%) and purification (6.7 fold). Initial protein concentration in the system did not show any specific trend on the partition behavior of the enzyme. The temperature at which the system is incubated did not show any significant (p ≥ 0.05) effect on enzyme partition and purification. Increasing the PEG concentration in the system from 15 to 25% resulted in reduction in enzyme yield from 53.7 to 21.9% and enzyme purification from 5 fold to 1.4 fold in PEG rich upper phase. pH also had a significant (p < 0.05) effect on the partition of the enzyme to the upper phase with highest purification (3.4 fold) at pH 9.0 and higher enzyme yield (46.2%) at pH 10.

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Recovery of value‐added globular proteins from tannery wastewaters using PEG – salt aqueous two‐phase systems

Saravanan

Rao

Murugesan

et al. 2006

J of Chemical Tech & Biotech

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Leather processing involves discharge of high-value soluble globular proteins in the wastewater. The recovery of value-added products from the wastewaters is gaining more importance in the context of recovery of wealth from waste. The recovery of these globular proteins from tannery wastewater was selected as a practical model system to study the implementation of polyethylene glycol (PEG)-sulfate aqueous two-phase systems (ATPS). The partition coefficient of bovine serum albumin is comparable to that of soluble proteins from tannery wastewaters. The influence of concentration of polymer, salt, pH and temperature on the partitioning of soluble proteins from tannery wastewaters has been studied. The PEG6000 + sodium sulfate + water system provide better partitioning of these soluble proteins as compared to PEG6000 + ammonium sulfate system. The maximum protein recovery yield for PEG6000 + sodium sulfate + water system at 20• C is 92.75%. The influence of temperature indicates the recovery of proteins from tannery wastewater to be better at lower temperature. The findings of these studies raise the potential application of ATPS processes for protein recovery from complex biological systems.

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The influence of salts on the phase composition in aqueous two-phase systems: experiments and predictions

Cited by 46 publications

References 17 publications

Application of aqueous mixtures of polypropylene glycol or polyethylene glycol with salts in proteomic analysis

Application of aqueous mixtures of polypropylene glycol or polyethylene glycol with salts in proteomic analysis

Purification of alkaline protease from chicken intestine by aqueous two phase system of polyethylene glycol and sodium citrate

Recovery of value‐added globular proteins from tannery wastewaters using PEG – salt aqueous two‐phase systems

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