{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T03:11:24Z","timestamp":1788318684704,"version":"build-2803163510"},"reference-count":60,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2024,10,17]],"date-time":"2024-10-17T00:00:00Z","timestamp":1729123200000},"content-version":"vor","delay-in-days":16,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["analyticalsciencejournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Cell Biochemistry &amp;amp; Function"],"published-print":{"date-parts":[[2024,10]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>Laccase is a copper\u2010containing polyphenol oxidase that can oxidize phenolic and non\u2010phenolic organic substrates. In the past decades, laccases had received considerable attention because of the ability to degrade various organic substances. Based on the codon preference of the <jats:italic>Pichia pastoris<\/jats:italic> expression system, this study optimized the gene structure of the laccase gene <jats:italic>Lcc1<\/jats:italic> from <jats:italic>Coprius cinerea<\/jats:italic> through synthetic biology methods. A new gene <jats:italic>Lcc1I<\/jats:italic> was synthesized and heterologously expressed in <jats:italic>P. pastoris<\/jats:italic>. After 3 days of cultivation in a shake flask at 30\u00b0C, the transformants produced at a yield of 890\u2009mg\u2009L<jats:sup>\u22121<\/jats:sup>protein. The highest production level of the recombinant laccase was 2760\u2009U\u2009L<jats:sup>\u22121<\/jats:sup>. The molecular mass of the recombinant laccase was estimated at 60\u2009kDa. The enzyme showed highest activity at pH 3.4 and 45\u00b0C. It possessed better stability at higher pH and lower temperature condition. Using 2,2'\u2010azino\u2010bis\u2010(3\u2010ethylbenzothiazoline)\u22126\u2010sulphonate (ABTS) as the substrate, the <jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub> and <jats:italic>V<\/jats:italic><jats:sub>max<\/jats:sub> values were 0.136\u2009mM and 9778\u2009\u03bcM\u2009min<jats:sup>\u22121<\/jats:sup>\u2009mg<jats:sup>\u22121<\/jats:sup>, respectively. The recombinant laccase could directly oxidize some triphenylmethane dyes like leuco\u2010crystal violet (LCV) and leuco\u2010malachite green (LMG). With the help of ABTS mediator, it could oxidize and degrade 77.7% crystal violet (CV) and 79.2% malachite green (MG) within 1\u2009h. Our results indicate that optimization of the laccase gene achieves good expression results in the host system. The dye degradation model constructed in this study may also be applied to the degradation of other organic pollutants and toxic substances, providing new solutions for environmental remediation against the increasingly severe environmental pollution.<\/jats:p>","DOI":"10.1002\/cbf.4127","type":"journal-article","created":{"date-parts":[[2024,10,18]],"date-time":"2024-10-18T02:24:03Z","timestamp":1729218243000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Characterization and Degradation of Triphenylmethane Dyes and Their Leuco\u2010Derivatives by Heterologously Expressed Laccase From <i>Coprinus cinerea<\/i>"],"prefix":"10.1002","volume":"42","author":[{"ORCID":"https:\/\/orcid.org\/0009-0005-8507-0466","authenticated-orcid":false,"given":"Cen","family":"Qian","sequence":"first","affiliation":[{"name":"Shanghai Key Laboratory of Agricultural Genetics and Breeding Biotechnology Research Institute, Shanghai 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