Discovery and Characterization of a 5-Hydroxymethylfurfural Oxidase from Methylovorus sp. Strain MP688

Dijkman, Willem P.; Fraaije, Marco W.

doi:10.1128/aem.03740-13

Cited by 129 publications

(210 citation statements)

References 28 publications

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“…Thus, it attacks the benzylic position of substituted aromatic heterocycles (such as HMF and DFF) in the same way as the respective position in the substituted aromatic carbocycles previously considered to be typical AAO substrates [7]. The newly identified activities of fungal AAO are similar to those of a bacterial HMF oxidase recently described in a Methylovorus species [30,31] results in the inability of AAO to catalyze the last step in the reaction cascade, which is successfully catalyzed by UPO.…”

Section: Discussionsupporting

confidence: 53%

5‐hydroxymethylfurfural conversion by fungal aryl‐alcohol oxidase and unspecific peroxygenase

Ferreira²,

et al. 2015

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Oxidative conversion of 5-hydroxymethylfurfural (HMF) is of biotechnological interest for the production of renewable (lignocellulose-based) platform chemicals, such as 2,5-furandicarboxylic acid (FDCA). To the best of our knowledge, the ability of fungal aryl-alcohol oxidase (AAO) to oxidize HMF is reported here for the first time, resulting in almost complete conversion into 2,5-formylfurancarboxylic acid (FFCA) in a few hours. The reaction starts with alcohol oxidation, yielding 2,5-diformylfuran (DFF), which is rapidly converted into FFCA by carbonyl oxidation, most probably without leaving the enzyme active site. This agrees with the similar catalytic efficiencies of the enzyme with respect to oxidization of HMF and DFF, and its very low activity on 2,5-hydroxymethylfurancarboxylic acid (which was not detected by GC-MS). However, AAO was found to be unable to directly oxidize the carbonyl group in FFCA, and only modest amounts of FDCA are formed from HMF (most probably by chemical oxidation of FFCA by the H 2 O 2 previously generated by AAO). As aldehyde oxidation by AAO proceeds via the corresponding geminal diols (aldehyde hydrates), the various carbonyl oxidation rates may be related to the low degree of hydration of FFCA compared with DFF. The conversion of HMF was completed by introducing a fungal unspecific heme peroxygenase that uses the H 2 O 2 generated by AAO to transform FFCA into FDCA, albeit more slowly than the previous AAO reactions. By adding this peroxygenase when FFCA production by AAO has been completed, transformation of HMF into FDCA may be achieved in a reaction cascade in which O 2 is the only co-substrate required, and water is the only byproduct formed.

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Section: Discussionsupporting

confidence: 53%

5‐hydroxymethylfurfural conversion by fungal aryl‐alcohol oxidase and unspecific peroxygenase

Ferreira²,

et al. 2015

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“…All tested BVMOs except BVMO02 showed significant activity towards furfural. From the BVMOs that showed the highest activities, we selected PAMOM446G for further biocatalytic exploration, as this enzyme is highly thermostable and solvent tolerant [22]. In fact, for the same reason we also included wild-type PAMO as it still displayed activity on furfural and it is known to exhibit differences in enantio-and regioselectivity when compared with PAMOM446G [20].…”

Section: Exploring Bvmos For Activity On Furfural and Hmfmentioning

confidence: 99%

“…Also, 12 mM phosphate buffer at pH 7.0 and 100% acetonitrile were used as mobile phases A and B respectively. A previously established HPLC method for the separation of furanoid compounds was used [22]. Reference compounds were used to identify and quantify the products.…”

Section: Product Identification Using Hplcmentioning

confidence: 99%

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Conversion of Furans by Baeyer-Villiger Monooxygenases

Kumar

Fraaije

2017

Catalysts

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Various furans are considered as valuable platform chemicals as they can be derived from plant biomass. Yet, for their exploitation, follow-up chemistry is required. Here we demonstrate that Baeyer-Villiger monooxygenases (BVMOs) can be used as biocatalysts for the selective oxidation of several furans, including 5-(hydroxymethyl) furfural (HMF) and furfural. A total of 15 different BVMOs were tested for their activity on furfural, which revealed that most of the biocatalysts were active on this aromatic aldehyde. Phenylacetone monooxygenase (PAMO) and a mutant thereof (PAMO M446G ) were selected for studying their biocatalytic potential in converting furfural and some other furans. While BVMOs are usually known to form an ester or lactone as a 'normal' product by inserting an oxygen atom adjacent to the carbonyl carbon of the substrate, our results reveal that both biocatalysts produce furanoid acids as the main product from the corresponding aldehydes. Altogether, our study shows that BVMOs can be employed for the selective oxidation of furans.

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“…[6] Thep rominent lipase Bf rom Candida antarctica catalyzes the enantioselective hydrolysis of thioesters (Scheme 1a). [10] In addition to its ability to produce the polymer building block 2,5-furandicarboxylic acid from 5-(hydroxylmethyl)furfural, [11] HFMO is able to oxidize abroad range of electronically activated benzylic and cinnamic primary alcohols, [10] and its variants transform sec-alcohols in as tereo-preferred fashion. [7] Flavoprotein oxidases,w hich are well established for the dioxygen-dependent oxidation of alcohols to carbonyl moieties, [8] were recently shown to catalyze the transformation of primary thiols into the corresponding thiocarbonyl analogues.…”

mentioning

confidence: 99%

Kinetic Resolution ofsec‐Thiols by Enantioselective Oxidation with Rationally Engineered 5‐(Hydroxymethyl)furfural Oxidase

et al. 2018

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Various flavoprotein oxidases were recently shown to oxidize primary thiols. Herein, this reactivity is extended to sec-thiols by using structure-guided engineering of 5-(hydroxymethyl)furfural oxidase (HMFO). The variants obtained were employed for the oxidative kinetic resolution of racemic sec-thiols, thus yielding the corresponding thioketones and nonreacted R-configured thiols with excellent enantioselectivities (E≥200). The engineering strategy applied went beyond the classic approach of replacing bulky amino acid residues with smaller ones, as the active site was additionally enlarged by a newly introduced Thr residue. This residue established a hydrogen-bonding interaction with the substrates, as verified in the crystal structure of the variant. These strategies unlocked HMFO variants for the enantioselective oxidation of a range of sec-thiols.

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Discovery and Characterization of a 5-Hydroxymethylfurfural Oxidase from Methylovorus sp. Strain MP688

Cited by 129 publications

References 28 publications

5‐hydroxymethylfurfural conversion by fungal aryl‐alcohol oxidase and unspecific peroxygenase

5‐hydroxymethylfurfural conversion by fungal aryl‐alcohol oxidase and unspecific peroxygenase

Conversion of Furans by Baeyer-Villiger Monooxygenases

Kinetic Resolution ofsec‐Thiols by Enantioselective Oxidation with Rationally Engineered 5‐(Hydroxymethyl)furfural Oxidase

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