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Production of Pharmaceuticals

Production of Pharmaceuticals

Industrial insulin production uses genetically engineered E. coli expressing a proinsulin gene controlled by a tryptophan promoter and containing a methionine linker for later cleavage. The cells also carry ampicillin resistance for selective growth. Seed cultures are stored at −80 °C and production begins by thawing a small amount to inoculate starter cultures, which are progressively scaled to a 50,000-L bioreactor. In the bioreactor, E. coli grow in nutrient-rich media under sterile, tightly...

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The MultiBac Protein Complex Production Platform at the EMBL

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Published on: July 11, 2013

Magnetic Multi-Enzymatic System for Cladribine Manufacturing.

Guillermo Cruz¹, Laura Pilar Saiz¹, Muhammad Bilal²

¹Applied Biotechnology Group, Universidad Europea de Madrid, Urbanización El Bosque, Calle Tajo, s/n, 28670 Villaviciosa de Odón, Spain.

International Journal of Molecular Sciences

|November 11, 2022

Summary

This study developed a reusable magnetic biocatalyst system for efficient cladribine synthesis. The novel enzyme cascade improved synthesis yield and converted by-products into valuable compounds.

Keywords:

cascade synthesis enzyme immobilization magnetic catalysts nucleoside analogues transglycosylation reaction

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Area of Science:

Biocatalysis and Enzyme Engineering
Sustainable Chemistry
Pharmaceutical Synthesis

Background:

Enzyme-mediated processes offer sustainable alternatives to traditional chemical synthesis.
Multi-enzymatic systems enhance complex synthetic pathways by minimizing by-products and overcoming reaction limitations.
Immobilizing enzymes on magnetic supports facilitates catalyst reusability and simplifies downstream processing.

Purpose of the Study:

To develop a novel cascade system for cladribine synthesis using immobilized enzymes.
To optimize magnetic biocatalysts for efficient and sustainable pharmaceutical production.
To evaluate the reusability and efficiency of the developed enzyme system.

Main Methods:

Immobilization of purine 2'-deoxyribosyltransferase (LmPDT) and hypoxanthine phosphoribosyltransferase (EcHPRT) onto magnetic microspheres.
Biochemical characterization of magnetic biocatalyst derivatives (MLmPDT3 and MEcHPRT3).
Application of the MLmPDT3/MEcHPRT3 system for one-pot cladribine synthesis.

Main Results:

Optimized magnetic biocatalysts MLmPDT3 and MEcHPRT3 demonstrated high activity and stability.
The MLmPDT3/MEcHPRT3 system achieved a 1.67-fold improvement in cladribine synthesis compared to MLmPDT3 alone.
The system efficiently converted an undesired by-product into a high-added-value product (90% conversion of Hyp into IMP).
The magnetic biocatalyst system retained 75% activity after 16 reuse cycles.

Conclusions:

The developed magnetic biocatalyst cascade system provides an efficient and sustainable method for cladribine synthesis.
Enzyme immobilization on magnetic supports enhances catalyst reusability and process efficiency.
This approach offers a greener alternative for pharmaceutical manufacturing by minimizing waste and maximizing product value.