Biocatalytic Syntheis of L‐Pipecolic Acid by a Lysine Cyclodeaminase: Batch and Flow Reactors

Stalder, Kaja; Benitez-Mateos, Ana I.; Paradisi, Francesca (2024). Biocatalytic Syntheis of L‐Pipecolic Acid by a Lysine Cyclodeaminase: Batch and Flow Reactors. ChemCatChem, 16(12) WILEY-VCH 10.1002/cctc.202301671

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L-Pipecolic Acid (L-PA) is a valuable building block for the
synthesis of pharmaceuticals such as anesthetics and
immunosuppressants. Thus, more efficient and greener strategies are
desired for its production. Herein, we have applied a previously
engineered variant of the Lysine Cyclodeaminase from Streptomyces
pristinaespiralis (e-SpLCD) for the bioconversion of L-Lysine into L-PA.
The reaction can be performed by the free e-SpLCD reaching full
conversion to 50 mM L-PA. From a biotechnological perspective, the
process scale-up has been trialed in a SpinChem® reactor, albeit with
lower conversion yields. To further enhance the biocatalyst stability,
we present a detailed study of the e-SpLCD immobilization on
microparticles. This enabled the integration of the immobilized
biocatalyst into a packed-bed reactor for the continuous flow synthesis
of L-PA. The full conversion was achieved in 90 min, maintaining also
high operational stability. Remarkably, the addition of exogenous
cofactor was not needed for the flow reaction, although the long-term
operational stability was improved by the addition of NAD+.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP)

UniBE Contributor:

Benitez Mateos, Ana Isabel, Paradisi, Francesca

Subjects:

500 Science > 540 Chemistry

ISSN:

1867-3880

Publisher:

WILEY-VCH

Funders:

[UNSPECIFIED] SNSF

Language:

English

Submitter:

Francesca Paradisi

Date Deposited:

15 Apr 2024 13:03

Last Modified:

25 Jun 2024 00:13

Publisher DOI:

10.1002/cctc.202301671

BORIS DOI:

10.48350/195704

URI:

https://boris.unibe.ch/id/eprint/195704

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