Rapid enzyme stabilization by computationally designed libraries of HMF oxidase
September 24-28, 2017
HMF oxidase (HMFO) from Methylovorus sp. is a recently characterized flavoprotein oxidase . HMFO is able to oxidize 5-(hydroxymethyl)furfural (HMF) into 2,5-furandicarboxylic acid (FDCA). Because HMF can be formed from fructose or other sugars and FDCA is a polymer building block, the oxidase has attracted attention as industrially relevant biocatalyst. The dicarboxylic acid FDCA can be polymerized with ethylene glycol to produce polyethylene furanoate (PEF). This renewable and bio-based polyester can be a valid alternative to the petroleum-based polyethylene terephthalate (PET) thanks to its similar characteristics.
HMFO is a promising biocatalyst for various oxidations and not only for the production of FDCA. The first step to the development of an HMFO with improved catalytic properties is the engineering of the enzyme to enhance its thermostability using the recently developed FRESCO method
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Caterina Martin, Marco W. Fraaije, and Hein Weijma, "Rapid enzyme stabilization by computationally designed libraries of HMF oxidase" in "Enzyme Engineering XXIV", Pierre Monsan, Toulouse White Biotechnology, France Magali Remaud-Simeon, LISBP-INSA, University of Toulouse, France Eds, ECI Symposium Series, (2017). http://dc.engconfintl.org/enzyme_xxiv/78