TY  - JOUR
AB  - 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.
DA  - 2020
DO  - 10.1002/cbic.201900648
LA  - eng
IS  - 14
M2  - 1968
PY  - 2020
SN  - 1439-4227
SP  - 1968-1971
T2  - Chembiochem : a European journal of chemical biology
TI  - Learning about Enzyme Stability against Organic Co-Solvents from Structural Insights by Ion Mobility Mass Spectrometry.
UR  - https://nbn-resolving.org/urn:nbn:de:0070-pub-29410861
Y2  - 2024-11-21T22:13:51
ER  -