EconPapers    
Economics at your fingertips  
 

Solvent concentration at 50% protein unfolding may reform enzyme stability ranking and process window identification

Frieda A. Sorgenfrei, Jeremy J. Sloan, Florian Weissensteiner, Marco Zechner, Niklas A. Mehner, Thomas L. Ellinghaus, Doreen Schachtschabel, Stefan Seemayer () and Wolfgang Kroutil ()
Additional contact information
Frieda A. Sorgenfrei: Austrian Centre of Industrial Biotechnology c/o University of Graz
Jeremy J. Sloan: BASF SE
Florian Weissensteiner: Austrian Centre of Industrial Biotechnology c/o University of Graz
Marco Zechner: Austrian Centre of Industrial Biotechnology c/o University of Graz
Niklas A. Mehner: BASF SE
Thomas L. Ellinghaus: BASF SE
Doreen Schachtschabel: BASF SE
Stefan Seemayer: BASF SE
Wolfgang Kroutil: Austrian Centre of Industrial Biotechnology c/o University of Graz

Nature Communications, 2024, vol. 15, issue 1, 1-11

Abstract: Abstract As water miscible organic co-solvents are often required for enzyme reactions to improve e.g., the solubility of the substrate in the aqueous medium, an enzyme is required which displays high stability in the presence of this co-solvent. Consequently, it is of utmost importance to identify the most suitable enzyme or the appropriate reaction conditions. Until now, the melting temperature is used in general as a measure for stability of enzymes. The experiments here show, that the melting temperature does not correlate to the activity observed in the presence of the solvent. As an alternative parameter, the concentration of the co-solvent at the point of 50% protein unfolding at a specific temperature T in short $${c}_{{U}_{50}}^{T}$$ c U 50 T is introduced. Analyzing a set of ene reductases, $${c}_{{U}_{50}}^{T}$$ c U 50 T is shown to indicate the concentration of the co-solvent where also the activity of the enzyme drops fastest. Comparing possible rankings of enzymes according to melting temperature and $${c}_{{U}_{50}}^{T}$$ c U 50 T reveals a clearly diverging outcome also depending on the specific solvent used. Additionally, plots of $${c}_{{U}_{50}}$$ c U 50 versus temperature enable a fast identification of possible reaction windows to deduce tolerated solvent concentrations and temperature.

Date: 2024
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-024-49774-0 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-49774-0

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-024-49774-0

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().

 
Page updated 2025-03-19
Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-49774-0