Evaluation of Driving Forces for Protein Partition in PEG-Salt Aqueous Two- Phase Systems and Optimization by Design of Experiments

Glyk, Anna; Solle, Dörte; Scheper, T.; Beutel, Sascha

doi:10.4172/2157-7064.1000389

Cited by 1 publication

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References 78 publications

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“…The addition of NaCl also generates an electric potential difference between the phases which can drive the migration of proteins towards one phase depending on their charge. Chloride ions are water structure breakers and partition predominantly to the PEG-rich phase (Glyk et al 2016). Thus, the PEG-rich phase becomes more negative when NaCl is added to the system and consequently, positively charged proteins migration is enhanced towards this phase (Andrews et al 2005;Rosa et al 2007).…”

Section: Effect Of Nacl Addition To Peg-potassium Phosphate Systems On the Recovery Of Mps And Plamentioning

confidence: 99%

Development of aqueous two-phase systems-based approaches for the selective recovery of metalloproteases and phospholipases A2 toxins from Crotalus molossus nigrescens venom

Enriquez-Ochoa

Meléndez‐Martínez

Aguilar‐Yáñez

et al. 2021

Bioresour. Bioprocess.

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Snake venoms are rich sources of proteins with potential biotechnological and pharmaceutical applications. Among them, metalloproteases (MPs) and phospholipases A2 (PLA2) are the most abundant. Their isolation involves a multistep chromatographic approach, which has proven to be effective, however implies high operating costs and long processing times. In this study, a cost-effective and simple method based on aqueous two-phase systems (ATPS) was developed to recover MPs and PLA2 from Crotalus molossus nigrescens venom. A system with PEG 400 g mol−1, volume ratio (VR) 1, tie line length (TLL) 25% w/w and pH 7 showed the best performance for PLA2 recovery. In systems with PEG 400 g mol−1, VR 1, TLL 15% w/w, pH 7 and 1 and 3% w/w of NaCl, selective recovery of MP subtype P-III was achieved; whereas, in a system with PEG 400 g mol−1, VR 1, TLL 25% w/w and pH 8.5, MP subtypes P-I and P-III were recovered. Due to their low costs, ethanol–salt systems were also evaluated, however, failed to differentially partition PLA2 and MPs. The use of ATPS could contribute to the simplification and cost reduction of protein isolation processes from snake venoms and other toxin fluids, as well as potentially aid their biochemical, proteomic and biological analyses. Graphic Abstract

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Section: Effect Of Nacl Addition To Peg-potassium Phosphate Systems On the Recovery Of Mps And Plamentioning

confidence: 99%

Development of aqueous two-phase systems-based approaches for the selective recovery of metalloproteases and phospholipases A2 toxins from Crotalus molossus nigrescens venom

Enriquez-Ochoa

Meléndez‐Martínez

Aguilar‐Yáñez

et al. 2021

Bioresour. Bioprocess.

View full text Add to dashboard Cite

show abstract

Evaluation of Driving Forces for Protein Partition in PEG-Salt Aqueous Two- Phase Systems and Optimization by Design of Experiments

Cited by 1 publication

References 78 publications

Development of aqueous two-phase systems-based approaches for the selective recovery of metalloproteases and phospholipases A2 toxins from Crotalus molossus nigrescens venom

Development of aqueous two-phase systems-based approaches for the selective recovery of metalloproteases and phospholipases A2 toxins from Crotalus molossus nigrescens venom

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