11-01: Bioproduction of 2,5-furandicarboxylic acid: from bacterial isolation to purified product

Furfural and 5-hydroxymethylfurfural (HMF) are potent fermentation inhibitors in lignocellulosic hydrolysates. The Gram negative bacterium Cupriavidus basilensis HMF14 can utilize furfural and HMF as sole carbon sources (1). The complete HMF and furfural degradation pathway of this bacterium was characterized, and the genes encoding enzymes in this pathway were identified (2). Expression of these genes in Pseudomonas putida enabled this organism to degrade both furfural and HMF, which provides promising leads for in situ removal of these inhibitors during microbial cultivation on lignocellulosic hydrolysate.

One of the enzymes involved in HMF degradation is an HMF/furfural oxidoreductase (HmfH), capable of converting HMF into the ‘green’ terephthalate-substitute 2,5-furandicarboxylic acid (FDCA). With this novel enzyme, an efficient whole-cell biocatalyst was developed for biotransformation of HMF into FDCA. In fed batch experiments using P. putida S12 expressing the hmfH gene, 30.8 g/l of FDCA was produced from HMF at a yield of 97%. FDCA was recovered from the culture broth as a 99.5% pure powder, at 76 % recovery, using acid precipitation and subsequent tetrahydrofuran extraction (3). These results provide a solid basis for the design of an efficient scaled-up bioprocess that will enable the development of FDCA as an important biobased building block.

References:

(1) N. Wierckx et al. 2010. Microbial. Biotechnol. 3: 336-343.

(2) F. Koopman et al. 2010. Proc. Nat. Acad. Sci. USA. 107: 4919-4924.

(3) F. Koopman et al. 2010. Biores. Tech. 101: 6291-6296.