Three‐Phasic Flow Bioreactor for Obtaining 5‐Formyl‐2‐Furancarboxylic Acid Catalyzed by an Immobilized Laccase Using Copper Sulfate as a Stabilizing Agent

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Authors: Nadia Guajardo, Karina Reichel, Mauricio Moncada‐Basualto
Cited by: 1
References: 50

Abstract

The effect of CuSO 4 on the stability of an immobilized laccase during the oxidation of HMF to FFCA was determined in a batch bioreactor and in a triphasic flow bioreactor. The enzyme was immobilized on a support functionalized with an epoxide and glyoxyl group; the latter achieved the highest immobilization yield by activity (87.5%). In batch oxidation of HMF catalyzed by laccase immobilized on a support with glyoxyl groups reached the highest conversion percentages (100%). In the biocatalyst stability, the addition of 20 mM CuSO 4 allowed achieving 50% HMF conversion at the end of the third cycle. In the absence of CuSO 4 , the biocatalyst was unable to catalyze the reaction. The oxidation in packed‐bed flow bioreactor resulted in the production of FFCA only. With CuSO 4 , the stability of the biocatalyst was maintained for 48 h, with a FFCA yield of 95%. The UM values (0.2–5 cm/min) demonstrated that above an air flow rate of 0.1 mL/min, there are no mass transfer problems affecting the reaction yield. The space‐time yield of FFCA (STY FFCA) (1.54 (mM/min)) was higher for the continuous system in the presence of CuSO 4 . Overall, this system provides a promising and scalable platform for sustainable industrial biocatalysis.

Fields of Study & Subjects

Enzyme-mediated dye degradation Enzyme Catalysis and Immobilization Biochemical and biochemical processes

Publication details

Journal / source
ChemPlusChem
Publisher
Wiley
Volume
91
Issue
1
Pages
e202500650–e202500650
Publication date
1 January 2026
Language
EN