000062839 001__ 62839
000062839 005__ 20210121114505.0
000062839 0247_ $$2doi$$a10.1111/febs.13177
000062839 0248_ $$2sideral$$a89931
000062839 037__ $$aART-2015-89931
000062839 041__ $$aeng
000062839 100__ $$aCarro, Juan
000062839 245__ $$a5-hydroxymethylfurfural conversion by fungal aryl-alcohol oxidase and unspecific peroxygenase
000062839 260__ $$c2015
000062839 5060_ $$aAccess copy available to the general public$$fUnrestricted
000062839 5203_ $$aOxidative 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 H2O2 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 H2O2 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 O2 is the only co-substrate required, and water is the only by-product formed.
000062839 536__ $$9info:eu-repo/grantAgreement/ES/MICINN/BIO2011-26694$$9info:eu-repo/grantAgreement/EC/FP7/613549/EU/Optimized oxidoreductases for medium and large scale industrial biotransformations/INDOX
000062839 540__ $$9info:eu-repo/semantics/openAccess$$aby-nc-nd$$uhttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
000062839 590__ $$a4.237$$b2015
000062839 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b72 / 289 = 0.249$$c2015$$dQ1$$eT1
000062839 592__ $$a2.152$$b2015
000062839 593__ $$aBiochemistry$$c2015$$dQ1
000062839 593__ $$aMolecular Biology$$c2015$$dQ1
000062839 593__ $$aCell Biology$$c2015$$dQ1
000062839 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000062839 700__ $$0(orcid)0000-0003-4076-6118$$aFerreira, Patricia$$uUniversidad de Zaragoza
000062839 700__ $$aRodríguez, Leonor
000062839 700__ $$aPrieto, Alicia
000062839 700__ $$aSerrano, Ana
000062839 700__ $$aBalcells, Beatriz
000062839 700__ $$aArdá, Ana
000062839 700__ $$aJiménez-Barbero, Jesús
000062839 700__ $$aGutiérrez, Ana
000062839 700__ $$aUllrich, René
000062839 700__ $$aHofrichter, Martín
000062839 700__ $$aMartínez, Ángel T.
000062839 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000062839 773__ $$g282, 16 (2015), 3218–3229$$pFEBS J.$$tFEBS JOURNAL$$x1742-464X
000062839 8564_ $$s887273$$uhttps://zaguan.unizar.es/record/62839/files/texto_completo.pdf$$yVersión publicada
000062839 8564_ $$s98314$$uhttps://zaguan.unizar.es/record/62839/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000062839 909CO $$ooai:zaguan.unizar.es:62839$$particulos$$pdriver
000062839 951__ $$a2021-01-21-10:53:57
000062839 980__ $$aARTICLE