Samenvatting
Various 4-alkylphenols can be easily obtained through reductive catalytic fractionation of lignocellulosic biomass. Selective dehydrogenation of 4-n-propylguaiacol results in the formation of isoeugenol, a valuable flavor and fragrance molecule and versatile precursor compound. Here we present the engineering of a bacterial eugenol oxidase to catalyze this reaction. Five mutations, identified from computational predictions, are first introduced to render the enzyme more thermostable. Other mutations are then added and analyzed to enhance chemoselectivity and activity. Structural insight demonstrates that the slow catalytic activity of an otherwise promising enzyme variant is due the formation of a slowly-decaying covalent substrate-flavin cofactor adduct that can be remedied by targeted residue changes. The final engineered variant comprises eight mutations, is thermostable, displays good activity and acts as a highly chemoselective 4-n-propylguaiacol oxidase. We lastly use our engineered biocatalyst in an illustrative preparative reaction at gram-scale. Our findings show that a natural enzyme can be redesigned into a tailored biocatalyst capable of valorizing lignin-based monophenols.
Originele taal-2 | English |
---|---|
Artikelnummer | 7195 |
Aantal pagina's | 12 |
Tijdschrift | Nature Communications |
Volume | 13 |
Nummer van het tijdschrift | 1 |
DOI's | |
Status | Published - 23-nov.-2022 |
Vingerafdruk
Duik in de onderzoeksthema's van 'Structure- and computational-aided engineering of an oxidase to produce isoeugenol from a lignin-derived compound'. Samen vormen ze een unieke vingerafdruk.Pers/Media
-
Modified enzyme brings value to lignin monomers
29/11/2022 → 09/12/2022
8 items van Media-aandacht
Pers / media: Expert Comment › Popular
-
Modifiziertes Enzym veredelt Ligninmonomere
01/12/2022
1 item van Media-aandacht
Pers / media: Expert Comment › Popular
-
Aangepast enzym maakt bouwstenen lignine bruikbaar
01/12/2022
1 item van Media-aandacht
Pers / media: Expert Comment › Popular