Characteristics of invertase partitioned in poly(ethylene glycol)/magnesium sulfate aqueous two-phase system

Karkaş, Taylan; Önal, Seçil

doi:10.1016/j.bej.2011.11.005

Cited by 45 publications

(44 citation statements)

References 43 publications

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“…It is well known that biomolecules partition in ATPSs is obviously influenced by pH of the system and generally system pH affects the partitioning behavior of protein by changing the charge of the target protein. Also, it affects the ratio of the charged species present in the extract by altering the surface characteristics of the so-called species or the ion composition [32]. The highest PF top (19.42) was obtained in the system pH of 7.0 (Fig.…”

Section: Effects Of Independent Variables On the B-galactosidasementioning

confidence: 99%

Partitioning of β-galactosidase in aqueous two-phase systems containing polyethyleneglycol and phosphate salts

Khayati

Anvari

Shahidi

2015

Fluid Phase Equilibria

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Section: Effects Of Independent Variables On the B-galactosidasementioning

confidence: 99%

Partitioning of β-galactosidase in aqueous two-phase systems containing polyethyleneglycol and phosphate salts

Khayati

Anvari

Shahidi

2015

Fluid Phase Equilibria

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“…It was also observed that the volume exclusion effect seen by the PEG 8000 (g/mol) molecules was significantly more profound as compared with the salting out effects [37] and, hence, the protein molecules were seen at the partition mostly in the bottom phase.…”

Section: Resultsmentioning

confidence: 99%

“…This could be due to the volume exclusion effect of the PEG molecules on the biomaterials. Additionally, an increase in the viscosity and compact polymeric network formation could also affect this parameter as a result of using higher molecular weight PEG [37]. Under these circumstances, it has been observed that the proteins favor partitioning in the salt-rich phases or the sediments.…”

Section: Discussionmentioning

confidence: 99%

Response Surface Methodology Modelling of an Aqueous Two-Phase System for Purification of Protease from Penicillium candidum (PCA 1/TT031) under Solid State Fermentation and Its Biochemical Characterization

Alhelli

Manap

Mohammed

et al. 2016

IJMS

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Penicillium candidum (PCA 1/TT031) synthesizes different types of extracellular proteases. The objective of this study is to optimize polyethylene glycol (PEG)/citrate based on an aqueous two-phase system (ATPS) and Response Surface Methodology (RSM) to purify protease from Penicillium candidum (PCA 1/TT031). The effects of different PEG molecular weights (1500–10,000 g/mol), PEG concentration (9%–20%), concentrations of NaCl (0%–10%) and the citrate buffer (8%–16%) on protease were also studied. The best protease purification could be achieved under the conditions of 9.0% (w/w) PEG 8000, 5.2% NaCl, and 15.9% sodium citrate concentration, which resulted in a one-sided protease partitioning for the bottom phase with a partition coefficient of 0.2, a 6.8-fold protease purification factor, and a yield of 93%. The response surface models displayed a significant (p ≤ 0.05) response which was fit for the variables that were studied as well as a high coefficient of determination (R2). Similarly, the predicted and observed values displayed no significant (p > 0.05) differences. In addition, our enzyme characterization study revealed that Penicillium candidum (PCA 1/TT031) produced a slight neutral protease with a molecular weight between 100 and 140 kDa. The optimal activity of the purified enzyme occurred at a pH of 6.0 and at a temperature of 50 °C. The stability between different pH and temperature ranges along with the effect of chemical metal ions and inhibitors were also studied. Our results reveal that the purified enzyme could be used in the dairy industry such as in accelerated cheese ripening.

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“…Also, it affects the ratio of the charged species present in the extract by altering their surface characteristics or the ion composition. [36] The results showed that at system pH of 5 and 6, there was negligible change in protein partitioning (K p ) observed (i.e. 0.28 and 0.31, respectively).…”

Section: Effect Of Ph On Lipase Partitioningmentioning

confidence: 91%

Extraction of lipase fromRhizopus microsporusfermentation culture by aqueous two-phase partitioning

Anvari

2015

Biotechnology & Biotechnological Equipment

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The purification of a desired protein from the complex mixture of biomolecules in a fermentation broth is one of the main challenges in industrial-scale biotechnological processes. For partial purification of industrial enzymes, one possible approach is to use aqueous two-phase extraction (APTE) as a primary downstream processing step. In the present study, the feasibility of utilizing ATPE for the purification of lipase from Rhizopus microsporus fermentation culture was investigated. The effects of the phase composition and salt type, molecular weight of the polyethylene glycol (PEG), pH of the system, sample loading and addition of neutral salts on lipase partitioning were investigated at 24 C. In most of the examined aqueous two-phase systems (ATPSs), lipase showed affinity to the top phase. Optimum conditions for lipase purification were obtained in 20% PEG 2000/12% (NH 4 ) 2 SO 4 , with 5% Na 2 CO 3 addition at pH D 8 for 30% crude load. For the optimized ATPS, the recovery yield and purification factor in the top phase were determined to be 92.3% and 19.8, respectively.

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Characteristics of invertase partitioned in poly(ethylene glycol)/magnesium sulfate aqueous two-phase system

Cited by 45 publications

References 43 publications

Partitioning of β-galactosidase in aqueous two-phase systems containing polyethyleneglycol and phosphate salts

Partitioning of β-galactosidase in aqueous two-phase systems containing polyethyleneglycol and phosphate salts

Response Surface Methodology Modelling of an Aqueous Two-Phase System for Purification of Protease from Penicillium candidum (PCA 1/TT031) under Solid State Fermentation and Its Biochemical Characterization

Extraction of lipase fromRhizopus microsporusfermentation culture by aqueous two-phase partitioning

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