{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,15]],"date-time":"2026-04-15T07:23:46Z","timestamp":1776237826991,"version":"3.50.1"},"reference-count":57,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2026,4,8]],"date-time":"2026-04-08T00:00:00Z","timestamp":1775606400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,4,8]],"date-time":"2026-04-08T00:00:00Z","timestamp":1775606400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100000780","name":"Euroopa Komisjoni","doi-asserted-by":"publisher","award":["Grant 101054658"],"award-info":[{"award-number":["Grant 101054658"]}],"id":[{"id":"10.13039\/501100000780","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["chemistry-europe.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["ChemBioChem"],"published-print":{"date-parts":[[2026,4,14]]},"abstract":"<jats:p>\n                    Vanadium\u2013dependent haloperoxidases (VHPOs) are attractive biocatalysts for halofunctionalisation chemistry, but their routine use is frequently constrained by poor soluble recombinant expression. Here, we explore protein fusion as a construct\u2010level strategy to simultaneously improve soluble expression of the vanadium chloroperoxidase from\n                    <jats:italic>Curvularia inaequalis<\/jats:italic>\n                    (\n                    <jats:italic>Ci<\/jats:italic>\n                    VCPO) and enable in situ H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    generation via formate oxidase from\n                    <jats:italic>Aspergillus oryzae<\/jats:italic>\n                    (\n                    <jats:italic>Ao<\/jats:italic>\n                    FOx). A panel of\n                    <jats:italic>Ao<\/jats:italic>\n                    FOx\u2013\n                    <jats:italic>Ci<\/jats:italic>\n                    VCPO fusion designs was generated by varying enzyme orientation, linker length and linker architecture. Notably, fusion constructs displayed markedly increased haloperoxidase activity yields in crude lysates (up to ~9\u2010fold relative to non\u2010fused\n                    <jats:italic>Ci<\/jats:italic>\n                    VCPO), whereas\n                    <jats:italic>Ao<\/jats:italic>\n                    FOx activity decreased (approximately 36%\u201375%) compared to the individually expressed oxidase. A representative construct (\n                    <jats:italic>Ci<\/jats:italic>\n                    VCPO\u201310 aa flexible linker\u2013\n                    <jats:italic>Ao<\/jats:italic>\n                    FOx) catalysed formate\u2010driven bromination of activated arenes (phenol, thymol) and oxidative bromolactonisation of 4\u2010pentenoic acid in crude extracts, giving product distributions consistent with hypobromite\u2010mediated reactivity. Time\u2010course experiments revealed that product formation was concentrated in the first 2 h and subsequently declined. H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    \u2010spiking partially restored activity, and sustained turnover was observed in a hypohalite\u2010free sulfoxidation model reaction, implicating hypobromite\u2010mediated deactivation of the\n                    <jats:italic>Ao<\/jats:italic>\n                    FOx domain as a principal robustness\u2010limiting factor.\n                  <\/jats:p>","DOI":"10.1002\/cbic.70322","type":"journal-article","created":{"date-parts":[[2026,4,8]],"date-time":"2026-04-08T10:19:42Z","timestamp":1775643582000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Elevating Haloperoxidase Expression in\n                    <i>Escherichia coli<\/i>\n                    through Fusion with a Formate Oxidase"],"prefix":"10.1002","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0009-0009-9131-1675","authenticated-orcid":false,"given":"Angelique","family":"Pothuizen","sequence":"first","affiliation":[{"name":"Department of Biotechnology Delft University of Technology  Delft Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jacob M. 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