11/01/2023

A multiplex assay to assess the transaminase activity toward chemically diverse amine donors

Title: A multiplex assay to assess the transaminase activity toward chemically diverse amine donors
Authors:

Czarnievicz, N; Rubanu, MG; Iturralde, M; Albarran-Velo, J; Diamanti, E; Gotor Fernández, V; Skolimowski, M; López-Gallego, F.

Journal: ChemBiochem 2022. Advanced Article. DOI: 10.1002/cbic.202200614

The development of methods to engineer and immobilize Amine transaminases (ATAs) improving their functionality and operational stability is gaining momentum. Nowadays, the quest for robust, fast, and easy-to-use methods to screen the activity of large collections of transaminases, is essential. This work presents a novel and multiplex fluorescence-based kinetic assay to assess ATA activity using 4-dimethylamino-1-naphthaldehyde as an amine acceptor. The developed assay allows us to screen a battery of amine donors using free and immobilized ATAs from different microbial sources as biocatalysts. As a result, using chromatographic methods, 4-hydroxybenzylamine was identified as the best amine donor for the amination of hydroxy methyl furfural. Finally, we adapt this method to determine the apparent Michaelis-Menten parameters of a model immobilized ATA at the microscopic (single-particle) level. Our studies promote the use of this multiplex, multidimensional assay to screen ATAs for further improvement.