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  Cascade kinetics in an enzyme-loaded aqueous two-phase system

Pavlović, M., Plucinski, A., Zhang, J., Antonietti, M., Zeininger, L., & Schmidt, B. V. K. J. (2020). Cascade kinetics in an enzyme-loaded aqueous two-phase system. Langmuir, 36(6), 1401-1408. doi:10.1021/acs.langmuir.0c00186.

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 Creators:
Pavlović, Marko1, Author           
Plucinski, Alexander2, Author
Zhang, Jianrui2, Author           
Antonietti, Markus3, Author           
Zeininger, Lukas1, Author           
Schmidt, Bernhard V. K. J.2, Author           
Affiliations:
1Lukas Zeininger, Kolloidchemie, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_3179204              
2Bernhard Schmidt, Kolloidchemie, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_2149676              
3Markus Antonietti, Kolloidchemie, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863321              

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Free keywords: Salts; Peptides and proteins; Diffusion; Phosphates; Polymers
 Abstract: Macromolecular crowding plays a critical role in the kinetics of enzymatic reactions. Dynamic compartmentalization of biological components in living cells due to liquid-liquid phase separation represents an important cell regulatory mech-anism that can increase enzyme concentration locally and influence the diffusion of substrates. In the present study, we probed partitioning of two enzymes (horseradish-peroxidase and urate-oxidase) in a poly(ethylene glycol) (PEG) – dextran (Dex) aqueous two-phase system (ATPS) as a function of salt concentration and ion position in the Hofmeister series. Moreover, we investigated enzymatic cascade reactions and their kinetics within the ATPS, which revealed a strong influence of the ion hydration stemming from the background electrolyte on the partitioning coefficients of proteins following the Hofmeister series. As a result, we were able to realize cross-partitioning of two enzymes due to different protein net charges at a chosen pH. Our study reveals a strong dependency of the enzyme activity on the substrate type and crowding agent interaction on the final kinetics of enzymatic reactions in ATPS and therefore provides substantial implications en route towards dynamic regulation of reactivity in synthetic protocells.

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Language(s): eng - English
 Dates: 2020-01-242020
 Publication Status: Published in print
 Pages: -
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 Identifiers: DOI: 10.1021/acs.langmuir.0c00186
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Title: Langmuir
  Abbreviation : Langmuir
Source Genre: Journal
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Publ. Info: Columbus, OH : American Chemical Society
Pages: - Volume / Issue: 36 (6) Sequence Number: - Start / End Page: 1401 - 1408 Identifier: ISSN: 0743-7463