{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,30]],"date-time":"2026-08-30T03:33:38Z","timestamp":1788060818609,"version":"build-2784847793"},"reference-count":26,"publisher":"Walter de Gruyter GmbH","issue":"3-4","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2019,2,25]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>There is an increasing interest in the application of peroxygenases in biocatalysis, because of their ability to catalyse the oxyfunctionalisation reaction in a stereoselective fashion and with high catalytic efficiencies, while using hydrogen peroxide or organic peroxides as oxidant. However, enzymes belonging to this class exhibit a very low stability in the presence of peroxides. With the aim of bypassing this fast and irreversible inactivation, we study the use of a gradual supply of hydrogen peroxide to maintain its concentration at stoichiometric levels. In this contribution, we report a multienzymatic cascade for in situ generation of hydrogen peroxide. In the first step, in the presence of NAD<jats:sup>+<\/jats:sup> cofactor, formate dehydrogenase from <jats:italic>Candida boidinii<\/jats:italic> (FDH) catalysed the oxidation of formate yielding CO<jats:sub>2<\/jats:sub>. Reduced NADH was reoxidised by the reduction of the flavin mononucleotide cofactor bound to an old yellow enzyme homologue from <jats:italic>Bacillus subtilis<\/jats:italic> (YqjM), which subsequently reacts with molecular oxygen yielding hydrogen peroxide. Finally, this system was coupled to the hydroxylation of ethylbenzene reaction catalysed by an evolved peroxygenase from <jats:italic>Agrocybe aegerita<\/jats:italic> (r<jats:italic>Aae<\/jats:italic>UPO). Additionally, we studied the influence of different reaction parameters on the performance of the cascade with the aim of improving the turnover of the hydroxylation reaction.<\/jats:p>","DOI":"10.1515\/znc-2018-0137","type":"journal-article","created":{"date-parts":[[2018,10,31]],"date-time":"2018-10-31T09:03:17Z","timestamp":1540976597000},"page":"101-104","source":"Crossref","is-referenced-by-count":20,"title":["Multienzymatic in situ hydrogen peroxide generation cascade for peroxygenase-catalysed oxyfunctionalisation reactions"],"prefix":"10.1515","volume":"74","author":[{"given":"Milja","family":"Pesic","sequence":"first","affiliation":[{"name":"Department of Biotechnology , Delft University of Technology , van der Maasweg 9 , 2629HZ Delft , The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S\u00e9bastien Jean-Paul","family":"Willot","sequence":"additional","affiliation":[{"name":"Department of Biotechnology , Delft University of Technology , van der Maasweg 9 , 2629HZ Delft , The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elena","family":"Fern\u00e1ndez-Fueyo","sequence":"additional","affiliation":[{"name":"Department of Biotechnology , Delft University of Technology , van der Maasweg 9 , 2629HZ Delft , The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Florian","family":"Tieves","sequence":"additional","affiliation":[{"name":"Department of Biotechnology , Delft University of Technology , van der Maasweg 9 , 2629HZ Delft , The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miguel","family":"Alcalde","sequence":"additional","affiliation":[{"name":"Department of Biocatalysis , Institute of Catalysis, CSIC , 28049 Madrid , Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Frank","family":"Hollmann","sequence":"additional","affiliation":[{"name":"Department of Biotechnology , Delft University of Technology , van der Maasweg 9 , 2629HZ Delft , The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"374","published-online":{"date-parts":[[2018,10,31]]},"reference":[{"key":"2021062203220364634_j_znc-2018-0137_ref_001_w2aab3b7b9b1b6b1ab2b1b1Aa","doi-asserted-by":"crossref","unstructured":"Dong JJ, Fern\u00e1ndez-Fueyo EE, Hollmann F, Paul CE, Pesic M, Schmid S, et al. Biocatalytic oxidation reactions: a chemist\u2019s perspective. Angew Chem Int Ed 2018;57:9238\u201361.","DOI":"10.1002\/anie.201800343"},{"key":"2021062203220364634_j_znc-2018-0137_ref_002_w2aab3b7b9b1b6b1ab2b1b2Aa","doi-asserted-by":"crossref","unstructured":"Mart\u00ednez AT, Ruiz-Due\u00f1as FJ, Camarero S, Serrano A, Linde D, Lund H, et al. Oxidoreductases on their way to industrial biotransformations. Biotechnol Adv 2017;35:815\u201331.","DOI":"10.1016\/j.biotechadv.2017.06.003"},{"key":"2021062203220364634_j_znc-2018-0137_ref_003_w2aab3b7b9b1b6b1ab2b1b3Aa","doi-asserted-by":"crossref","unstructured":"Hofrichter M, Ullrich R. Oxidations catalyzed by fungal peroxygenases. Curr Opin Chem Biol 2014;19:116\u201325.","DOI":"10.1016\/j.cbpa.2014.01.015"},{"key":"2021062203220364634_j_znc-2018-0137_ref_004_w2aab3b7b9b1b6b1ab2b1b4Aa","doi-asserted-by":"crossref","unstructured":"Wang Y, Lan D, Durrani R, Hollmann F. Peroxygenases en route to becoming dream catalysts. 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