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Chembiochem. 2020 Jan 29. doi: 10.1002/cbic.201900648. [Epub ahead of print]

Learning about Enzyme Stability against Organic Co-Solvents from Structural Insights by Ion Mobility Mass Spectrometry.

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Bielefeld University, Faculty of Chemistry, GERMANY.
Universität Bielefeld, Fakultät für Chemie Organische Chemie I, Universitätsstr. 25, 33615, Bielefeld, GERMANY.


Ion mobility spectrometry (IMS) coupled with mass spectrometry (MS) enables the investigation of protein folding in solution. Herein we present a proof-of-concept for obtaining structural information about the folding of a protein in dependency of the amount of an organic co-solvent in the aqueous medium by means this IMS-MS method. By analyzing the protein with native nano-electrospray ionization (ESI)-IMS-MS, the impact of acetonitrile (ACN) as a representative organic co-solvent and/or pH values on the folding of an enzyme was successfully evaluated in a fast and straightforward fashion exemplified for an ene reductase from Gluconobacter oxydans. The IMS-MS results are in agreement with the findings from the NADPH-based spectrophotometric enzyme activity tests under analogous conditions, thus also rationalizing these "wet" analytical data. For this ene reductase, a higher tolerance against ACN in the presence of a buffer was observed by both analytical methods. The results suggest that this IMS-MS methodology could be a useful complementary tool to existing methods in process optimization and fine tuning of solvent conditions for biotransformations.


Ene reductase; Enzyme catalysis; Ion mobility spectrometry; Mass spectrometry; Protein structure


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