Activation and Stabilization of Engineered Amine Dehydrogenase by Fatty Acids for Bioprocess Intensification of Asymmetric Reductive Amination

Journal Article (2025)
Author(s)

Weixi Kong (Hebei Vocational University of Technology and Engineering, Hebei University of Technology)

Jiawang Zhang (Hebei University of Technology)

Liya Zhou (Hebei University of Technology)

Guanhua Liu (Hebei University of Technology)

Ying He (Hebei University of Technology)

Li Ma (Hebei University of Technology)

Frank Hollmann (TU Delft - BT/Biocatalysis)

Lihui Wang (Tianjin Modern Vocational Technology College)

Yunting Liu (Hebei University of Technology)

Yanjun Jiang (Hebei University of Technology)

DOI related publication
https://doi.org/10.1021/acscatal.4c05904 Final published version
More Info
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Publication Year
2025
Language
English
Bibliographical Note
Green Open Access added to TU Delft Institutional Repository 'You share, we take care!' - Taverne project https://www.openaccess.nl/en/you-share-we-take-care Otherwise as indicated in the copyright section: the publisher is the copyright holder of this work and the author uses the Dutch legislation to make this work public.
Journal title
ACS Catalysis
Issue number
1
Volume number
15
Pages (from-to)
34-43
Downloads counter
519
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Abstract

In this study, we present a significant advancement in the field of enzymatic asymmetric reductive amination (ARA) of ketones, a pivotal reaction for chiral amine synthesis. Through a combination of semirational enzyme design and bioprocess development, we achieve the dual activation and stabilization of amine dehydrogenase (AmDH) to meet industrial demands. The engineered AmDH exhibits remarkable catalytic efficiency (turnover number, TON >1,000,000) and exceptional stability (half-life >7 days at 50 °C), with a broadened substrate scope including various aryl alkyl ketones and fatty ketones. Leveraging biobased oleic acid as an activator and stabilizer, we achieved kilogram-scale synthesis of chiral amines. Furthermore, the integration of AmDH with chemical catalysts in chemoenzymatic cascades has enabled the synthesis of a wide array of pharmaceutically relevant amines from diverse substrates, demonstrating the enzyme’s versatility and potential to transform synthetic chemistry.

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