Mediated, Amperometric Biosensor for Glucose-6-Phosphate Monitoring Based on Entrapped Glucose-6-Phosphate Dehydrogenase, Mg2+Ions, Tetracyanoquinodimethane, and Nicotinamide Adenine Dinucleotide Phosphate in Carbon Paste

Bassi, Amarjeet; Tang, Diqing; Bergougnou, M.A.

doi:10.1006/abio.1998.3082

Cited by 24 publications

(19 citation statements)

References 10 publications

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“…The enzyme studied in this paper, glucose-6-phosphate dehydrogenase (G6PD) (EC.1.1.1.49), is the first enzyme of the pentose phosphate pathway and is very interesting as an analytical reagent, being used in various quantitative assays, including the measurement of creatin-kinase activity, hexoses concentrations, and as a marker for enzyme immunoassays (Bassi et al, 1999;Lojudice et al, 2001). The industrial purification of the hydrophilic enzyme G6PD involves expensive techniques, such as affinity chromatography and ion-exchange chromatography (Champluvier and Kula, 1992;Chang and Chase, 1996;McCreath et al, 1995), making the search for a simpler and m ore economical method to purify G6PD important and desirable.…”

Section: Spherical Micelle Cylindrical Micelle Bilayermentioning

confidence: 99%

Two-phase aqueous micellar systems: an alternative method for protein purification

Rangel-Yagui

Pessoa

Blankschtein

2004

Braz. J. Chem. Eng.

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-Two-phase aqueous micellar systems can be exploited in separation science for the extraction/purification of desired biomolecules. This article reviews recent experimental and theoretical work by Blankschtein and co-workers on the use of two-phase aqueous micellar systems for the separation of hydrophilic proteins. The experimental partitioning behavior of the enzyme glucose-6-phosphate dehydrogenase (G6PD) in two-phase aqueous micellar systems is also reviewed and new results are presented. Specifically, we discuss very recent work on the purification of G6PD using: i) a two-phase aqueous micellar system composed of the nonionic surfactant n-decyl tetra(ethylene oxide) (C 10 E 4 ), and (ii) a two-phase aqueous mixed micellar system composed of C 10 E 4 and the cationic surfactant decyltrimethylammonium bromide (C 10 TAB). Our results indicate that the two-phase aqueous mixed (C 10 E 4 /C 10 TAB) micellar system can improve significantly the partitioning behavior of G6PD relative to that observed in the two-phase aqueous C 10 E 4 micellar system.

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Section: Spherical Micelle Cylindrical Micelle Bilayermentioning

confidence: 99%

Two-phase aqueous micellar systems: an alternative method for protein purification

Rangel-Yagui

Pessoa

Blankschtein

2004

Braz. J. Chem. Eng.

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“…We also investigated the partitioning of a model protein, the enzyme glucose-6-phosphate dehydrogenase (G6PD), in ATPMS composed of C 10 E 4 with and without salt addition. G6PD is obtaind by bioprocess and presents great interest as an analytical reagent, being used in various quantitative assays, including the measurement of creatin-kinase activity, hexose concentrations, and as a biomarker in enzyme immunoassays (Bassi et al, 1999;Lojudice et al, 2001). Therefore, ATPMS coud be an alternative for this biomolecule extraction/purification.…”

Section: Introductionmentioning

confidence: 99%

Influence of salts on the coexistence curve and protein partitioning in nonionic aqueous two-phase micellar systems

Lopes

Santos-Ebinuma

Pessoa

et al. 2014

Braz. J. Chem. Eng.

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-Aqueous two-phase micellar systems (ATPMS) can be exploited in separation science for the extraction/purification of desired biomolecules. Prior to phase separation the surfactant solution reaches a cloud point temperature, which is influenced by the presence of electrolytes. In this work, we provide an investigation on the cloud point behavior of the nonionic surfactant C 10 E 4 in the presence of NaCl, Li 2 SO 4 and KI. We also investigated the salts' influence on a model protein partitioning. NaCl and Li 2 SO 4 promoted a depression of the cloud point. The order of salts and the concentration that decreased the cloud point was: Li 2 SO 4 0.5 M > NaCl 0.5 M ≈ Li 2 SO 4 0.2 M. On the other hand, 0.5 M KI dislocated the curve to higher cloud point values. For our model protein, glucose-6-phosphate dehydrogenase (G6PD), partitioning experiments with 0.5 M NaCl or 0.2 M Li 2 SO 4 at 13.85 °C showed similar results, with K G6PD ~ 0.46. The lowest partition coefficient was obtained in the presence of 0.5 M KI (K G6PD = 0.12), with major recovery of the enzyme in the micelle-dilute phase (%Recovery = 90%). Our results show that choosing the correct salt to add to ATPMS may be useful to attain the desired partitioning conditions at more extreme temperatures. Furthermore, this system can be effective to separate a target biomolecule from fermented broth contaminants.

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“…The enzyme G6PD, presents great interest as analytical reagent, being used in various quantitative assays, including the measurement of creatin-kinase activity, hexoses concentrations, and as a marker for enzyme immunoassays. 23,24 …”

Section: Introductionmentioning

confidence: 99%

Can affinity interactions influence the partitioning of glucose-6-phosphate dehydrogenase in two-phase aqueous micellar systems?

Lopes¹,

Pessoa²,

Rangel-Yagui³

2008

Quím. Nova

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Recebido em 8/2/07; aceito em 27/11/07; publicado na web em 8/7/08In this work, we provide an investigation of the role and strength of affinity interactions on the partitioning of the glucose-6-phosphate dehydrogenase in aqueous two-phase micellar systems. These systems are constituted of micellar surfactant solutions and offer both hydrophobic and hydrophilic environments, providing selectivity to biomolecules. We studied G6PD partitioning in systems composed of the nonionic surfactants, separately, in the presence and absence of affinity ligands. We observed that G6PD partitions to the micelle-poor phase, owing to the strength of excluded-volume interactions in these systems that drive the protein to the micellepoor phase, where there is more free volume available.

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Mediated, Amperometric Biosensor for Glucose-6-Phosphate Monitoring Based on Entrapped Glucose-6-Phosphate Dehydrogenase, Mg2+Ions, Tetracyanoquinodimethane, and Nicotinamide Adenine Dinucleotide Phosphate in Carbon Paste

Cited by 24 publications

References 10 publications

Two-phase aqueous micellar systems: an alternative method for protein purification

Two-phase aqueous micellar systems: an alternative method for protein purification

Influence of salts on the coexistence curve and protein partitioning in nonionic aqueous two-phase micellar systems

Can affinity interactions influence the partitioning of glucose-6-phosphate dehydrogenase in two-phase aqueous micellar systems?

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