NADPH biosensor-based identification of an alcohol dehydrogenase variant with improved catalytic properties caused by a single charge reversal at the protein surface

NADPH biosensor-based identification of an alcohol dehydrogenase variant with improved catalytic properties caused by a single charge reversal at the protein surface

Abstract Alcohol dehydrogenases (ADHs) are used in reductive biotransformations for the production of valuable chiral alcohols. In this study, we used a high-throughput screening approach based on the NADPH biosensor pSenSox and fluorescence-activated cell sorting (FACS) to search for variants of th...

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Bibliographic Details
Main Authors: Alina Spielmann, Yannik Brack, Hugo van Beek, Lion Flachbart, Lea Sundermeyer, Meike Baumgart, Michael Bott
Format: Article
Language:English
Published: SpringerOpen 2020-01-01
Series:AMB Express
Subjects:
NADPH biosensor
Lactobacillus brevis
NADPH-dependent alcohol dehydrogenase
Enzyme optimization
Fluorescence-activated cell sorting
Random mutagenesis
Online Access:https://doi.org/10.1186/s13568-020-0946-7

Internet

https://doi.org/10.1186/s13568-020-0946-7

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