Synthetic activity of recombinant whole cell biocatalysts containing 2‐deoxy‐D‐ribose‐5‐phosphate aldolase from Pectobacterium atrosepticum

VARELA, ROMINA FERNÁNDEZ; VALINO, ANA LAURA; ABDELRAHEEM, EMAN; MÉDICI, ROSARIO; SAYÉ, MELISA; PEREIRA, CLAUDIO A.; HAGEDOORN, PETER-LEON; HANEFELD, ULF; IRIBARREN, ADOLFO; LEWKOWICZ, ELIZABETH SANDRA

CHEMBIOCHEM

WILEY-V C H VERLAG GMBH

Año: 2022

1439-4227

In nature 2-deoxy-D-ribose-5-phosphate aldolase (DERA) catalyzes 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 for decrease cholesterol level 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 analyzed. 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 what makes it suitable for industrial applications.