{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,11]],"date-time":"2026-03-11T17:37:23Z","timestamp":1773250643061,"version":"3.50.1"},"reference-count":55,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2025,5,4]],"date-time":"2025-05-04T00:00:00Z","timestamp":1746316800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["iubmb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Biotech and App Biochem"],"published-print":{"date-parts":[[2025,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Laccases are multicopper oxidases with numerous applications because of their wide substrate variety. The yeast surface display (YSD) technology is a powerful tool for the expression of recombinant laccases that can be used to design robust oxidative biocatalysts and combine stability and flexibility in a whole\u2010cell system. In order to gain insights on improving the laccase performance, we investigated the release, from the yeast's surface, of a recombinant laccase (OB1) from\n                    <jats:italic>Saccharomyces cerevisiae<\/jats:italic>\n                    EBY100's cell surface. The laccase, or derivatives thereof, was released as a fusion protein connected, by a flexible peptide linker, to a carrier protein (Aga2 adhesin). The optimum conditions for the release of the fused protein were determined by applying a 2\n                    <jats:sup>2<\/jats:sup>\n                    factorial experimental design, exploring biomass and dithiothreitol concentration as the variables. The released Aga2\u20103x(G4S)\u2010OB1 derivatives were biochemically characterized and compared to the whole\u2010cell system. Laccase variant TX13A\u2010OB1 was the best\u2010performing fusion protein out of six variants, with a K\n                    <jats:sub>m<\/jats:sub>\n                    value of 0.0137\u00a0\u00b1\u00a00.0032\u00a0mM and V\n                    <jats:sub>max<\/jats:sub>\n                    0.0075\u00a0\u00b1\u00a00.0001 (\u00b5mol\u00a0min\n                    <jats:sup>\u22121<\/jats:sup>\n                    ) for ABTS. All variants showed thermostability at 60\u00b0C and retained over 50% relative activity within a pH range of 3\u20135, compared to the parental protein. No significant differences in oxidation performance were determined with respect to the oxidation profile of gallic acid, vanillic acid, and catechol. On the other hand, there was an improvement in ferulic acid. Additionally, laccase relative activity remained above 60% in the presence of 10%\u201320 % ethanol for all variants. This research improved the stability of a recombinant laccase released from the yeast's cell surface carrying an engineered protein domain with adhesin properties, suggesting an influence from this domain on the laccase performance and the potential use of other adhesins for wider applications of laccases and other enzymes.\n                  <\/jats:p>","DOI":"10.1002\/bab.2768","type":"journal-article","created":{"date-parts":[[2025,5,5]],"date-time":"2025-05-05T01:55:05Z","timestamp":1746410105000},"page":"1633-1643","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Oxidation Performance of the Aga2\u2010Laccase Fusion Produced by Yeast Surface Display"],"prefix":"10.1002","volume":"72","author":[{"given":"Dulce Y.","family":"Arenas\u2010Olivares","sequence":"first","affiliation":[{"name":"Centro de Investigaci\u00f3n en Biotecnolog\u00eda Universidad Aut\u00f3noma del Estado de Morelos Morelos M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daniel","family":"Morales\u2010Guzm\u00e1n","sequence":"additional","affiliation":[{"name":"Centro de Investigaci\u00f3n en Biotecnolog\u00eda Universidad Aut\u00f3noma del Estado de Morelos Morelos M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Karla V.","family":"Teymennet\u2010Ram\u00edrez","sequence":"additional","affiliation":[{"name":"Centro de Investigaci\u00f3n en Biotecnolog\u00eda Universidad Aut\u00f3noma del Estado de Morelos Morelos M\u00e9xico"},{"name":"Department of Biocatalysis, Institute of Catalysis CSIC Madrid Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Miguel","family":"Alcalde","sequence":"additional","affiliation":[{"name":"Department of Biocatalysis, Institute of Catalysis CSIC Madrid Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M. 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