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

Sproß J, Yamashita Y, Gröger H (2020)
Chembiochem : a European journal of chemical biology.

Zeitschriftenaufsatz | E-Veröff. vor dem Druck | Englisch
 
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Abstract / Bemerkung
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. © 2020 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Erscheinungsjahr
2020
Zeitschriftentitel
Chembiochem : a European journal of chemical biology
eISSN
1439-7633
Page URI
https://pub.uni-bielefeld.de/record/2941086

Zitieren

Sproß J, Yamashita Y, Gröger H. Learning about Enzyme Stability against Organic Co-Solvents from Structural Insights by Ion Mobility Mass Spectrometry. Chembiochem : a European journal of chemical biology. 2020.
Sproß, J., Yamashita, Y., & Gröger, H. (2020). Learning about Enzyme Stability against Organic Co-Solvents from Structural Insights by Ion Mobility Mass Spectrometry. Chembiochem : a European journal of chemical biology. doi:10.1002/cbic.201900648
Sproß, J., Yamashita, Y., and Gröger, H. (2020). Learning about Enzyme Stability against Organic Co-Solvents from Structural Insights by Ion Mobility Mass Spectrometry. Chembiochem : a European journal of chemical biology.
Sproß, J., Yamashita, Y., & Gröger, H., 2020. Learning about Enzyme Stability against Organic Co-Solvents from Structural Insights by Ion Mobility Mass Spectrometry. Chembiochem : a European journal of chemical biology.
J. Sproß, Y. Yamashita, and H. Gröger, “Learning about Enzyme Stability against Organic Co-Solvents from Structural Insights by Ion Mobility Mass Spectrometry.”, Chembiochem : a European journal of chemical biology, 2020.
Sproß, J., Yamashita, Y., Gröger, H.: Learning about Enzyme Stability against Organic Co-Solvents from Structural Insights by Ion Mobility Mass Spectrometry. Chembiochem : a European journal of chemical biology. (2020).
Sproß, Jens, Yamashita, Yasunobu, and Gröger, Harald. “Learning about Enzyme Stability against Organic Co-Solvents from Structural Insights by Ion Mobility Mass Spectrometry.”. Chembiochem : a European journal of chemical biology (2020).

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