Hydroxyapatite as an Enzyme Carrier in Continuous-Flow Biocatalysis: An Improved Synthesis of γ-Glutamyl Derivatives

High Resolution Image Download MS PowerPoint Slide Biocatalysis has proved to be of great importance to pursue a more sustainable production of fine chemicals, and enzyme immobilization is a crucial tool to achieve this goal. In this work, hydroxyapatite, an eco-friendly material, was used as a support for the immobilization of a γ-glutamyltransferase from Escherichia coli, an enzyme that catalyzes the synthesis of bioactive γ-glutamyl derivatives, exploiting the noncovalent interactions between the support and the enzyme. After screening the immobilization conditions, the storage (up to 90 days) and the thermal stability (50 °C) of the obtained immobilized biocatalyst were studied, as well as its reuse in up to 10 consecutive reactions of γ-glutamylation of S -allyl- l -cysteine, to give γ- l -glutamyl- S -allyl- l -cysteine ( 3 ), a flavor enhancer occurring in garlic extract. Finally, the immobilized enzyme was used to prepare a packed-bed reactor and 3 was synthesized under continuous-flow conditions improving both the productivity (from 19.4 to 35.1 μmol·h –1 ) and the space-time yield (9.7 vs 381 μmol·h –1 ·mL –1 ) of the reaction.

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Journal
Organic Process Research & Development
Published
2026-06-19
DOI
https://doi.org/10.1021/acs.oprd.6c00083
Primary Topic
Enzyme Catalysis and Immobilization
Type
article
Field-Weighted Citation Impact
0.00

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article

Hydroxyapatite as an Enzyme Carrier in Continuous-Flow Biocatalysis: An Improved Synthesis of γ-Glutamyl Derivatives

Carlo F. Morelli, Antonella Gervasini, Giovanna Speranza, Marco Rabuffetti et al.
Organic Process Research & Development
Enzyme Catalysis and Immobilization
article

Hydroxyapatite as an Enzyme Carrier in Continuous-Flow Biocatalysis: An Improved Synthesis of γ-Glutamyl Derivatives

Carlo F. Morelli, Antonella Gervasini, Giovanna Speranza, Marco Rabuffetti, Cinzia Calvio, Maurizio Benaglia, Sebastiano Campisi, Fabrizio Medici, Leonardo Gelati
article en

Abstract

High Resolution Image Download MS PowerPoint Slide Biocatalysis has proved to be of great importance to pursue a more sustainable production of fine chemicals, and enzyme immobilization is a crucial tool to achieve this goal. In this work, hydroxyapatite, an eco-friendly material, was used as a support for the immobilization of a γ-glutamyltransferase from Escherichia coli, an enzyme that catalyzes the synthesis of bioactive γ-glutamyl derivatives, exploiting the noncovalent interactions between the support and the enzyme. After screening the immobilization conditions, the storage (up to 90 days) and the thermal stability (50 °C) of the obtained immobilized biocatalyst were studied, as well as its reuse in up to 10 consecutive reactions of γ-glutamylation of S -allyl- l -cysteine, to give γ- l -glutamyl- S -allyl- l -cysteine ( 3 ), a flavor enhancer occurring in garlic extract. Finally, the immobilized enzyme was used to prepare a packed-bed reactor and 3 was synthesized under continuous-flow conditions improving both the productivity (from 19.4 to 35.1 μmol·h –1 ) and the space-time yield (9.7 vs 381 μmol·h –1 ·mL –1 ) of the reaction.

Organic Process Research & Development
University of Milan (IT), University of Pavia (IT), University of Campania "Luigi Vanvitelli" (IT)
NextGenerationEU
Clean water and sanitation
Openalex Percentile: Top 11%
Enzyme Catalysis and Immobilization
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