2,5-Furandicarboxaldehyde as a bio-based crosslinking agent replacing glutaraldehyde for covalent enzyme immobilization

Danielli, Chiara; Langen, Luuk van; Boes, Deborah M; Asaro, Fioretta; Anselmi, Serena; Provenza, Francesca; Renzi, Monia; Gardossi, Lucia

doi:10.1039/d2ra07153c

Cited by 22 publications

(14 citation statements)

References 30 publications

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“…A recent study showed that DFF can be used instead of glutaraldehyde as a crosslinking molecule in enzyme immobilization [39] . In that case, the immobilization of glucoamylase was performed on a polymethylmethacrylate support, where the resin was activated with DFF in buffer.…”

Section: Resultsmentioning

confidence: 99%

“…A recent study showed that DFF can be used instead of glutaraldehyde as a crosslinking molecule in enzyme immobilization. [39] In that case, the immobilization of glucoamylase was performed on a polymethylmethacrylate support, where the resin was activated with DFF in buffer. To assess whether adsorption of HMF or DFF to the carrier could occur, these chemicals were incubated with ECR8215F (epoxy) in 0.1 M NaPi buffer pH 7.4 and ethyl acetate (EtOAc) (Figure 2).…”

Section: Oxidation Of Hmf To Dff In Different Water-containing Ethyl ...mentioning

confidence: 99%

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Selective Oxidation of 5‐Hydroxymethylfurfural to 2,5‐Diformylfuran in Biphasic Media using Immobilized Galactose Oxidase: Proof of Concept and Limitations

Milić,

Byström,

Domínguez de María

et al. 2024

ChemCatChem

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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 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 H2O, the reaction was conducted at 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.

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Section: Resultsmentioning

confidence: 99%

Section: Oxidation Of Hmf To Dff In Different Water-containing Ethyl ...mentioning

confidence: 99%

Selective Oxidation of 5‐Hydroxymethylfurfural to 2,5‐Diformylfuran in Biphasic Media using Immobilized Galactose Oxidase: Proof of Concept and Limitations

Milić,

Byström,

Domínguez de María

et al. 2024

ChemCatChem

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“…Glucoamylase is an essential and high‐yield enzyme product widely used in the industrial production of alcohol, vinegar, starch, sugar, and so on (Qi et al., 2022). Free glucoamylase has poor stability, inactivation, heat, and acid resistance, whereas the emergence of immobilization technology has effectively improved the environmental tolerance of free glucoamylase (Danielli et al., 2022).…”

Section: Introductionmentioning

confidence: 99%

Preparation of layer‐assembled W/O/W‐type microencapsulated beads and application in solid‐state fermentation

Wen,

Jiang,

Zheng

et al. 2024

Journal of Food Science

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In this study, microcapsule beads‐0–3‐layers (M‐0–3 indicates microencapsulated beads with 0, 1, 2, and 3 layers) were prepared, their properties were measured and characterized, and the effects of M‐0–3 on solid‐state fermentation were investigated. The results showed that in a liquid environment, the releasing glucoamylase activities of M‐0–3 were 55.77%, 47.67%, 45.85%, and 42.87% in 360 h, respectively. In the solid environment, the reducing sugar production efficiency of M‐0–3 was 29.84%, 27.72%, 19.16%, and 15.93% in 15 days, respectively. Adding M‐0–3 improved the alcohol and reduced sugar content while decreasing the residual starch content of the Jiupei, indicating that adding M‐0–3 was beneficial to the solid‐state fermentation of Baijiu. Solid‐state fermentation simulation experiments illustrated that microcapsule beads play a positive role in the production of Baijiu, enhancing raw material utilization and yield of Baijiu production.

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“…HMF occurs naturally in products such as honey, toasted bread, or coffee [20,[30][31][32], and it can be synthesized from fructose, isomerized from glucose [33], or retrieved sustainably from food waste biomass [34,35]. DFF, which can be used as a crosslinker for enzyme immobilization [36], can be produced from fructose or glucose [37]. Both HMFA and DAF are relevant building blocks in the pharmaceutical industry.…”

Section: Introductionmentioning

confidence: 99%

Biosynthesis of Furfurylamines in Batch and Continuous Flow by Immobilized Amine Transaminases

et al. 2023

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Building blocks with amine functionality are crucial in the chemical industry. Biocatalytic syntheses and chemicals derived from renewable resources are increasingly desired to achieve sustainable production of these amines. As a result, renewable materials such as furfurals, especially furfurylamines like 5-(hydroxymethyl)furfurylamine (HMFA) and 2,5-di(aminomethyl)furan (DAF), are gaining increasing attention. In this study, we identified four different amine transaminases (ATAs) that catalyze the reductive amination of 5-(hydroxymethyl)furfural (HMF) and 2,5-diformylfuran (DFF). We successfully immobilized these ATAs on glutaraldehyde-functionalized amine beads using multiple binding and on amine beads by site-selective binding of the unique Cα-formylglycine within an aldehyde tag. All immobilized ATAs were efficiently reused in five repetitive cycles of reductive amination of HMF with alanine as co-substrate, while the ATA from Silicibacter pomeroyi (ATA-Spo) also exhibited high stability for reuse when isopropylamine was used as an amine donor. Additionally, immobilized ATA-Spo yielded high conversion in the batch syntheses of HMFA and DAF using alanine (87% and 87%, respectively) or isopropylamine (99% and 98%, respectively) as amine donors. We further demonstrated that ATA-Spo was effective for the reductive amination of HMF with alanine or isopropylamine in continuous-flow catalysis with high conversion up to 12 days (48% and 41%, respectively).

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2,5-Furandicarboxaldehyde as a bio-based crosslinking agent replacing glutaraldehyde for covalent enzyme immobilization

Abstract: The bio-based 2,5-furandicarboxaldehyde (diformylfuran, DFF) proved as effective as glutaraldehyde in the covalent immobilization of enzymes on amino-functionalized carriers. The binding is attributed to stable imine bond formation.

Cited by 22 publications

References 30 publications

Selective Oxidation of 5‐Hydroxymethylfurfural to 2,5‐Diformylfuran in Biphasic Media using Immobilized Galactose Oxidase: Proof of Concept and Limitations

Selective Oxidation of 5‐Hydroxymethylfurfural to 2,5‐Diformylfuran in Biphasic Media using Immobilized Galactose Oxidase: Proof of Concept and Limitations

Preparation of layer‐assembled W/O/W‐type microencapsulated beads and application in solid‐state fermentation

Biosynthesis of Furfurylamines in Batch and Continuous Flow by Immobilized Amine Transaminases

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