Structural and Partitioning Studies of Bovine Serum Albumin in Mixture of (Poly(ethylene glycol) + K2HPO4 + H2O)

Faravash, Ram Sanati; Modarress, Hamid; Nasernejad, Bahram

doi:10.1021/je060235b

Cited by 11 publications

(13 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…That is what we call the salting-out effect, when you salt something, the salt molecules move from the bottom up and this happens to the proteins as well. In contrast to what is shown in this work, [40] and [41] had a conflicted opinion when they concluded that increasing PEG concentration levels had a beneficial effect on Rec% and K which are increased according to PEG increment. The most hydrophobic anions or cations will tend to spread out in the most hydrophobic phase, while co-ions, which are less hydrophobic, will spread out in the hydrophilic phase.…”

Section: Concentration Effect Of Pegcontrasting

confidence: 99%

“…After pH 8 the system lost the two-phase formation and specifically in pH 8.3. [22,25,31,40,44,47,48] all had a good agreement with our investigation, while [20,49] had different results according to their studies for different ATPS systems. They went with an opinion that negatively charged protein molecules partition to the bottom phase at high pH, because of the negative net charge of the protein, which has a pI of 4.7.…”

Section: Ph Effectsupporting

confidence: 79%

“…In this study, it was found that the optimum proportion of PEG to (Dextran/SPH) was 1.5 g/10 ml of PEG to 2.4 g/10 ml of (Dextran/SPH). This result was convenient to [20,23,40,41,44], and there were no incompatible opinions found.…”

Section: Concentration Effect Of Salt/dextranmentioning

confidence: 71%

See 2 more Smart Citations

Application of Aqueous Two-Phase Systems in the Extraction of Bovine Serum Albumin

Mahdi¹,

Hameed²,

Ali³

2023

JOPC

View full text Add to dashboard Cite

Protein partitioning in an Aqueous Two-Phase System (ATPS) has been found to be a powerful method for extracting and separating mixtures of biomolecules. In Aqueous Two-Phase Systems, many factors influence the Partition coefficient (K) (which is the ratio of protein concentration in the top phase to that in the bottom phase) and the Recovery percent (Rec%). Two systems of ATPS were used: first, polyethylene glycol (PEG4000)/sodium phosphate (SPH), and second, PEG4000/Dextran. The behavior of Rec% and (K) of pure Bovine Serum Albumin (BSA) in (ATPS) has been investigated throughout the study of the effects of five parameters: (temperature (T), the concentration of polyethylene glycol (PEG4000), the concentration of sodium phosphate or Dextran, pH, and the addition of sodium chloride as a supporting agent). In both systems, pH was the more significant parameter on a Recovery percent (Rec%) and partition coefficient (K). In the first system, the maximum (Rec%) and (K) was 98.08% and 50.99, respectively, at a temperature of 31°C, the concentration of PEG4000 of 1.5 g/10 ml, the concentration of sodium phosphate at 2.4 g/10 ml, pH 10, and the concentration of NaCl at 0.5 M. While in the second system, the parameter that has a more significant effect on (Rec%) and (K) was the temperature. The maximum (Rec%) and (K) were 97.54% and 39.7 respectively at a temperature of 31°C, with a concentration of PEG4000 1.5 g/10 ml, the concentration of Dextran 2.4 g/10 ml, pH 5, and concentration of NaCl at 0.1 M.

show abstract

Section: Concentration Effect Of Pegcontrasting

confidence: 99%

Section: Ph Effectsupporting

confidence: 79%

See 1 more Smart Citation

Application of Aqueous Two-Phase Systems in the Extraction of Bovine Serum Albumin

Mahdi¹,

Hameed²,

Ali³

2023

JOPC

View full text Add to dashboard Cite

show abstract

“…In these works, they found that the partitioning of these two enzymes largely depends on the weight fractions of polymer and salt in feed as well as the molecular weight of polymer; however, the temperature has very limited effect on their partitioning. Faravash et al conducted structural and partitioning studies of bovine serum albumin in an ATPS of PEG2000 + K 2 HPO 4 + H 2 O, and the results indicate that the partition coefficient of this biomolecule increases with the increase in the tie-line length (TLL) of ATPS. Taghavivan and Pazuki investigated the cefalexin partitioning in biocompatible ATPS formed by Tween 20 and different inorganic salts (MgSO 4 and Na 2 SO 4 )/organic salt (Na 3 C 6 H 5 O 7 ).…”

Section: Introductionmentioning

confidence: 99%

Optimal Design of Aqueous Two-Phase Systems for Biomolecule Partitioning

Chen

Kontogeorgis

2023

Ind. Eng. Chem. Res.

View full text Add to dashboard Cite

Aqueous two-phase systems (ATPS) have exhibited superior performance in many biotechnological applications. To promote the implementation of these powerful platforms by industry in the downstream processing, an optimal design method is developed to tailor high-performance ATPS for partitioning biomolecules in this work. In this design method, two machine learning (ML) models that combine the artificial neural network (ANN) algorithm and group contribution (GC) method are respectively employed to predict the phase equilibrium composition of polymer-electrolyte ATPS and the partition of biomolecules in these aqueous systems. By integrating these two ANN-GC models into the computer-aided design technique, the optimal ATPS is identified by solving an optimization-based mixed-integer non-linear programming (MINLP) problem. As a proof of concept, results of partitioning cefazolin and β-amylase are presented. In the case of cefazolin, the partitioning performance of our tailored ATPS (PPG600 + KNaSO4 + H2O) is nearly 7 times greater than that of the reported ATPS (PEG6000 + Na3C6H5O7 + H2O). Meanwhile, the ATPS of PPG600 + KNaSO4 + H2O gives a cefazolin recovery of 95.0 wt % and an agent input of 0.154 kg/kg aqueous solution, and for the ATPS of PEG6000 + Na3C6H5O7 + H2O, these values are 90.6 and 0.233, respectively. For the second case, the partition coefficient of β-amylase in our proposed ATPS (PPG400 + KNaHPO4 + H2O) is about 13.5 times higher than that of the reported ATPS (PEG10000 + KH2PO4 + H2O). In addition, the ATPS of PPG600 + KNaSO4 + H2O gives an β-amylase recovery of 97.3 wt % at a cost of 0.387 kg agent input/kg aqueous solution, and for the ATPS of PEG6000 + Na3C6H5O7 + H2O, they are 66.3 and 0.252, respectively.

show abstract

“…Studies [10][11][12][13][14][15] show that protein distribution is a function of diverse factors such as: polymer molar mass, polymer concentrations, pH, ionic species, hydrophobic groups and temperature. The study of these operational variables is necessary for the design and scale increase of separation processes.…”

Section: Introductionmentioning

confidence: 99%