Details
| Original language | English |
|---|---|
| Article number | e202301384 |
| Journal | CHEMCATCHEM |
| Volume | 16 |
| Issue number | 4 |
| Early online date | 22 Dec 2023 |
| Publication status | Published - 22 Feb 2024 |
Abstract
The oxidation of 5-hydroxymethylfurfural (HMF) to 2,5-diformylfuran (DFF) is a key reaction in valorizing biomass. DFF is hardly soluble in water, while HMF is often obtained from biorefineries in crude wet organic fractions. Thus, the reaction is challenging for both biocatalysis performed in aqueous media, and for chemocatalysis where the presence of water often results in catalyst poisoning. Galactose oxidase (GalOx) can selectively oxidize HMF to DFF and displays promising activity in aqueous-organic media. In this study, GalOx was immobilized on ten carriers, assessing the immobilization yield, activity, and stability. Covalently immobilized GalOx catalyzed the oxidation of HMF to DFF in neat and water-saturated EtOAc, and in biphasic systems of various water contents. At 50 % v/v H 2O, the reaction was conducted at a semi-preparative scale (50 mL) with no adverse effect on DFF yield. Some limitations arise, such as enzyme deactivation, and adsorption of DFF to the support, particularly in the aqueous fraction. Future options to upgrade the route may include designed stable enzymes under the presence of HMF/DFF, and the setup of microaqueous systems where DFF adsorption is minimized. The use of wet EtOAc media would be a promising approach in future biorefineries employing inexpensive crude wet organic fractions.
Keywords
- 5-hydroxymethylfurfural (HMF), biocatalysis, biphasic systems, enzyme immobilization, galactose oxidase
ASJC Scopus subject areas
- Chemical Engineering(all)
- Catalysis
- Chemistry(all)
- Inorganic Chemistry
- Chemistry(all)
- Physical and Theoretical Chemistry
- Chemistry(all)
- Organic Chemistry
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In: CHEMCATCHEM, Vol. 16, No. 4, e202301384, 22.02.2024.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Selective Oxidation of 5‐Hydroxymethylfurfural to 2,5‐Diformylfuran in Biphasic Media using Immobilized Galactose Oxidase: Proof of Concept and Limitations
AU - Milić, Milica
AU - Byström, Emil
AU - María, Pablo Domínguez de
AU - Kara, Selin
N1 - Funding Information: . This project has received funding from the European Union's Horizon 2020 research and innovation program under the Marie Skłodowska‐Curie grant agreement No. 860414. The authors thank Dr. Alessandra Basso and Dr. Simona Serban from Purolite Ltd. for providing the Lifetech carriers, Assoc. Prof. Thomas Tørring and Thomas Dyekjær from the Department of Biological and Chemical Engineering at Aarhus University for their kind help with HPLC analyses. Open Access funding enabled and organized by Projekt DEAL TM
PY - 2024/2/22
Y1 - 2024/2/22
N2 - The oxidation of 5-hydroxymethylfurfural (HMF) to 2,5-diformylfuran (DFF) is a key reaction in valorizing biomass. DFF is hardly soluble in water, while HMF is often obtained from biorefineries in crude wet organic fractions. Thus, the reaction is challenging for both biocatalysis performed in aqueous media, and for chemocatalysis where the presence of water often results in catalyst poisoning. Galactose oxidase (GalOx) can selectively oxidize HMF to DFF and displays promising activity in aqueous-organic media. In this study, GalOx was immobilized on ten carriers, assessing the immobilization yield, activity, and stability. Covalently immobilized GalOx catalyzed the oxidation of HMF to DFF in neat and water-saturated EtOAc, and in biphasic systems of various water contents. At 50 % v/v H 2O, the reaction was conducted at a semi-preparative scale (50 mL) with no adverse effect on DFF yield. Some limitations arise, such as enzyme deactivation, and adsorption of DFF to the support, particularly in the aqueous fraction. Future options to upgrade the route may include designed stable enzymes under the presence of HMF/DFF, and the setup of microaqueous systems where DFF adsorption is minimized. The use of wet EtOAc media would be a promising approach in future biorefineries employing inexpensive crude wet organic fractions.
AB - The oxidation of 5-hydroxymethylfurfural (HMF) to 2,5-diformylfuran (DFF) is a key reaction in valorizing biomass. DFF is hardly soluble in water, while HMF is often obtained from biorefineries in crude wet organic fractions. Thus, the reaction is challenging for both biocatalysis performed in aqueous media, and for chemocatalysis where the presence of water often results in catalyst poisoning. Galactose oxidase (GalOx) can selectively oxidize HMF to DFF and displays promising activity in aqueous-organic media. In this study, GalOx was immobilized on ten carriers, assessing the immobilization yield, activity, and stability. Covalently immobilized GalOx catalyzed the oxidation of HMF to DFF in neat and water-saturated EtOAc, and in biphasic systems of various water contents. At 50 % v/v H 2O, the reaction was conducted at a semi-preparative scale (50 mL) with no adverse effect on DFF yield. Some limitations arise, such as enzyme deactivation, and adsorption of DFF to the support, particularly in the aqueous fraction. Future options to upgrade the route may include designed stable enzymes under the presence of HMF/DFF, and the setup of microaqueous systems where DFF adsorption is minimized. The use of wet EtOAc media would be a promising approach in future biorefineries employing inexpensive crude wet organic fractions.
KW - 5-hydroxymethylfurfural (HMF)
KW - biocatalysis
KW - biphasic systems
KW - enzyme immobilization
KW - galactose oxidase
UR - http://www.scopus.com/inward/record.url?scp=85182180319&partnerID=8YFLogxK
U2 - 10.1002/cctc.202301384
DO - 10.1002/cctc.202301384
M3 - Article
VL - 16
JO - CHEMCATCHEM
JF - CHEMCATCHEM
SN - 1867-3880
IS - 4
M1 - e202301384
ER -