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