Cascade Kinetics in an Enzyme-Loaded Aqueous Two-Phase System

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 mechanism that can increase enzyme concentration locally and influ...

Ausführliche Beschreibung

Bibliographische Detailangaben
Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 36(2020), 6 vom: 18. Feb., Seite 1401-1408
1. Verfasser: Pavlovic, Marko (VerfasserIn)
Weitere Verfasser: Plucinski, Alexander, Zhang, Jianrui, Antonietti, Markus, Zeininger, Lukas, Schmidt, Bernhard V K J
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2020
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Proteins Water 059QF0KO0R Polyethylene Glycols 3WJQ0SDW1A Horseradish Peroxidase EC 1.11.1.-
LEADER 01000naa a22002652 4500
001 NLM305739786
003 DE-627
005 20231225121835.0
007 cr uuu---uuuuu
008 231225s2020 xx |||||o 00| ||eng c
024 7 |a 10.1021/acs.langmuir.0c00186  |2 doi 
028 5 2 |a pubmed24n1019.xml 
035 |a (DE-627)NLM305739786 
035 |a (NLM)31977224 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Pavlovic, Marko  |e verfasserin  |4 aut 
245 1 0 |a Cascade Kinetics in an Enzyme-Loaded Aqueous Two-Phase System 
264 1 |c 2020 
336 |a Text  |b txt  |2 rdacontent 
337 |a ƒaComputermedien  |b c  |2 rdamedia 
338 |a ƒa Online-Ressource  |b cr  |2 rdacarrier 
500 |a Date Completed 21.06.2021 
500 |a Date Revised 21.06.2021 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a 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 mechanism 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)-dextran 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 because of 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 the ATPS and therefore provides substantial implications en route toward dynamic regulation of reactivity in synthetic protocells 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Proteins  |2 NLM 
650 7 |a Water  |2 NLM 
650 7 |a 059QF0KO0R  |2 NLM 
650 7 |a Polyethylene Glycols  |2 NLM 
650 7 |a 3WJQ0SDW1A  |2 NLM 
650 7 |a Horseradish Peroxidase  |2 NLM 
650 7 |a EC 1.11.1.-  |2 NLM 
700 1 |a Plucinski, Alexander  |e verfasserin  |4 aut 
700 1 |a Zhang, Jianrui  |e verfasserin  |4 aut 
700 1 |a Antonietti, Markus  |e verfasserin  |4 aut 
700 1 |a Zeininger, Lukas  |e verfasserin  |4 aut 
700 1 |a Schmidt, Bernhard V K J  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Langmuir : the ACS journal of surfaces and colloids  |d 1992  |g 36(2020), 6 vom: 18. Feb., Seite 1401-1408  |w (DE-627)NLM098181009  |x 1520-5827  |7 nnns 
773 1 8 |g volume:36  |g year:2020  |g number:6  |g day:18  |g month:02  |g pages:1401-1408 
856 4 0 |u http://dx.doi.org/10.1021/acs.langmuir.0c00186  |3 Volltext 
912 |a GBV_USEFLAG_A 
912 |a SYSFLAG_A 
912 |a GBV_NLM 
912 |a GBV_ILN_22 
912 |a GBV_ILN_350 
912 |a GBV_ILN_721 
951 |a AR 
952 |d 36  |j 2020  |e 6  |b 18  |c 02  |h 1401-1408