Synthetic Activity of Recombinant Whole Cell Biocatalysts Containing 2-Deoxy-D-ribose-5-phosphate Aldolase from Pectobacterium atrosepticum

Journal article (2022)

Authors

Romina Fernández Varela Universidad Nacional de Quilmes, Bernal and Concet
Ana Laura Valino Universidad Nacional de Quilmes, Bernal and Concet
E.M.M. Abdelraheem BT/Biocatalysis - AS
R. Medici BT/Bioprocess Engineering - AS , BT/Biocatalysis - AS
Melisa Sayé Universidad de Buenos Aires
Claudio A. Pereira Universidad de Buenos Aires
P.L. Hagedoorn BT/Biocatalysis - AS
U. Hanefeld BT/Biocatalysis - AS
Adolfo Iribarren Universidad Nacional de Quilmes, Bernal and Concet
Elizabeth Lewkowicz Universidad Nacional de Quilmes, Bernal and Concet
Research Group
BT/Biocatalysis (AS) (TU Delft)
Copyright: © 2022 Romina Fernández Varela, Ana Laura Valino, E.M.M. Abdelraheem, R. Medici, Melisa Sayé, Claudio A. Pereira, P.L. Hagedoorn, U. Hanefeld, Adolfo Iribarren, Elizabeth Lewkowicz
DOI: https://doi.org/10.1002/cbic.202200147
More Info
expand_more

Published Date

2022

Language

English

Reuse Rights

Other than for strictly personal use, it is not permitted to download, forward or distribute the text or part of it, without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license such as Creative Commons.

Faculty

Applied Sciences

Department

BT/Biotechnologie

Research Group

BT/Biocatalysis

Abstract

In nature 2-deoxy-D-ribose-5-phosphate aldolase (DERA) catalyses the reversible formation of 2-deoxyribose 5-phosphate from D-glyceraldehyde 3-phosphate and acetaldehyde. In addition, this enzyme can use acetaldehyde as the sole substrate, resulting in a tandem aldol reaction, yielding 2,4,6-trideoxy-D-erythro-hexapyranose, which spontaneously cyclizes. This reaction is very useful for the synthesis of the side chain of statin-type drugs used to decrease cholesterol levels in blood. One of the main challenges in the use of DERA in industrial processes, where high substrate loads are needed to achieve the desired productivity, is its inactivation by high acetaldehyde concentration. In this work, the utility of different variants of Pectobacterium atrosepticum DERA (PaDERA) as whole cell biocatalysts to synthesize 2-deoxyribose 5-phosphate and 2,4,6-trideoxy-D-erythro-hexapyranose was analysed. Under optimized conditions, E. coli BL21 (PaDERA C-His AA C49M) whole cells yields 99 % of both products. Furthermore, this enzyme is able to tolerate 500 mM acetaldehyde in a whole-cell experiment which makes it suitable for industrial applications.

Files

ChemBioChem_2022_Varela_Synthe... (.pdf)
(.pdf | 0.541 Mb)
- Embargo expired in 01-07-2023