Enzyme‐Catalyzed Oxidation of 5‐Hydroxymethylfurfural to Furan‐2,5‐dicarboxylic Acid

Abstract

Furan-2,5-dicarboxylic acid (FDCA) is a biobased platform chemical for the production of polymers. In the past few years, numerous multistep chemical routes have been reported on the synthesis of FDCA by oxidation of 5-hydroxymethylfurfural (HMF). Recently we identified an FAD-dependent enzyme which is active towards HMF and related compounds. This oxidase has the remarkable capability of oxidizing [5-(hydroxymethyl)furan-2-yl]methanol to FDCA, a reaction involving four consecutive oxidations. The oxidase can produce FDCA from HMF with high yield at ambient temperature and pressure. Examination of the underlying mechanism shows that the oxidase acts on alcohol groups only and depends on the hydration of aldehydes for the oxidation reaction required to form FDCA.

Conversion of Furans by Baeyer-Villiger Monooxygenases

“…Only a few biocatalytic or fermentative methods have been described for the production of FDCA starting from HMF. A bacterial flavoprotein oxidase was shown to be capable of performing the complete oxidation of HMF into FDCA [8,9]. Similar results were obtained by using a combination of two or more enzymes [10,11].…”

“…HPLC methods were derived from previous studies in our laboratory [9,22]. Calibration curves for the substrates and possible products (furfural, 2-furoic acid, HMF, DFF, 5-hydroxymethyl-2-furancarboxylic acid (HMFCA), FFA and FDCA) were determined beforehand.…”

Ligninolytic enzymes: a biotechnological alternative for bioethanol production

“…This type of detoxification is performed by aryl-alcohol oxidase (AAO) which is a less investigated group of ligninolytic enzymes. AAO have been assessed in the degradation of 5-hydroxymethylfurfural (HMF) and polyunsaturated alcohols [99][100][101]. Carro et al [101] evaluated the transformation of HMF into 2,5-furandicarboxylic acid (FDCA) by AAO catalysis.…”

Mechanistic and biocatalytic enzymology of flavoprotein oxidases

“…alcohol [4-(3-hydroxyprop-1-en-1-yl)-2-methoxyphenol], the first step in its degradation (44,45). The sequences of these proteins reveal that they belong to the 4PO subfamily, showing highest similarity to PCMH, and they are predicted to contain 8α-O--tyrosyl-FAD as a cofactor.…”

“…Higher plants typically contain multiple genes encoding CKXs, with the best studied CKX families being those from Arabidopsis thaliana (seven isoforms) and Z. mays (thirteen isoforms). The various members of these families differ in terms of their tissuespecific expression patterns, (predicted) subcellular localisation and substrate specificity, suggesting they have distinct functions in vivo (43)(44)(45)(46)(47). The crystal structure of ZmCKX1 revealed that the substrate binding site consists of an internal cavity, where the isoprenoid or aromatic side chain of the substrate binds, linked to the surface through a narrow pore (48).…”