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Laccases offer a promising biodegradation route but suffer from low secretion yield and poor stability. This study characterized a novel Priestia megaterium laccase PmL and adopted a dual engineering strategy. A 222-sequence Pichia pastoris signal peptide library was constructed, and the optimal SP4 signal peptide elevated the extracellular activity of PmL to 2.94-fold of \u03b1-factor signal peptide, reaching 435.0 U\/mL. Further PROSS computational design generated mutant SP4-M1, which simultaneously enhanced extracellular secretion (587.3 vs 147.9 U\/mL) and thermostability (half-life at 80 \u00b0C: 423.7 vs 126.9 min) compared to PmL. Mycotoxin degradation assays confirmed SP4-M1 efficacy, achieving 99.5% degradation of aflatoxin B1 (AFB1) and 100% of zearalenone (ZEN). This systematic engineering strategy effectively optimizes the laccase performance, providing a reliable biocatalytic approach for mycotoxin contamination mitigation.<\/jats:p>","DOI":"10.1021\/acs.jafc.6c05915","type":"journal-article","created":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T06:01:59Z","timestamp":1787032919000},"page":"26684-26698","source":"Crossref","is-referenced-by-count":0,"title":["Optimization of\nLaccase PmL Secretion and Thermal\nStability via Calculation-Guided Design for Mycotoxin Degradation"],"prefix":"10.1021","volume":"74","author":[{"given":"Yuanyuan","family":"Zhe","sequence":"first","affiliation":[{"name":"Yunnan Normal University , , , ,","place":["Kunming, Yunnan, China, 650500"]},{"name":"Yunnan Normal University , , , ,","place":["Kunming, Yunnan, China, 650500"]},{"name":"Yunnan Normal University , , , ,","place":["Kunming, Yunnan, China, 650500"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuxi","family":"Jin","sequence":"additional","affiliation":[{"name":"Yunnan Normal University , , , ,","place":["Kunming, Yunnan, China, 650500"]},{"name":"Yunnan Normal University , , , ,","place":["Kunming, Yunnan, China, 650500"]},{"name":"Yunnan Normal University , , , ,","place":["Kunming, Yunnan, China, 650500"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yutong","family":"Gao","sequence":"additional","affiliation":[{"name":"Yunnan Normal University , , , ,","place":["Kunming, Yunnan, China, 650500"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9789-1596","authenticated-orcid":true,"given":"Nanyu","family":"Han","sequence":"additional","affiliation":[{"name":"Yunnan Normal University , , , ,","place":["Kunming, Yunnan, China, 650500"]},{"name":"Yunnan Normal University , , , ,","place":["Kunming, Yunnan, China, 650500"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7998-3673","authenticated-orcid":true,"given":"Zunxi","family":"Huang","sequence":"additional","affiliation":[{"name":"Yunnan Normal University , , , ,","place":["Kunming, Yunnan, China, 650500"]},{"name":"Yunnan Normal University , , , ,","place":["Kunming, Yunnan, China, 650500"]},{"name":"Yunnan Normal University , , , ,","place":["Kunming, Yunnan, China, 650500"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,18]]},"reference":[{"issue":"4","key":"2026090104472290500_cit1","doi-asserted-by":"publisher","first-page":"233","DOI":"10.1002\/jbt.20284","article-title":"Comparative\nstudy of toxic effects of zearalenone and its two major metabolites\n\u03b1-zearalenol and \u03b2-zearalenol on cultured human Caco-2\nCells","volume":"23","author":"Abid-Essefi","year":"2009","journal-title":"J. Biochem. Mol. Toxicol."},{"key":"2026090104472290500_cit2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cofs.2025.101306","article-title":"Mycotoxins Hazard:\nThe European View","volume":"63","author":"Pinton","year":"2025","journal-title":"Curr. Opin. Food Sci."},{"issue":"1","key":"2026090104472290500_cit3","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1186\/s40643-021-00484-1","article-title":"Laccases\nas green and versatile biocatalysts:\nfrom lab to enzyme market\u2500an overview","volume":"8","author":"Brugnari","year":"2021","journal-title":"Bioresour. Bioprocess."},{"issue":"44","key":"2026090104472290500_cit4","doi-asserted-by":"publisher","first-page":"24158","DOI":"10.1021\/acs.jafc.4c06669","article-title":"Laccase: a\ngreen biocatalyst offers immense potential for food industrial and\nbiotechnological applications","volume":"72","author":"Zhai","year":"2024","journal-title":"J. Agric. Food\nChem."},{"issue":"23","key":"2026090104472290500_cit5","doi-asserted-by":"publisher","first-page":"13371","DOI":"10.1021\/acs.jafc.4c01304","article-title":"Thermo-alkali-tolerant\nrecombinant laccase from Bacillus Swezeyi and its\ndegradation potential against zearalenone\nand aflatoxin B1","volume":"72","author":"Mwabulili","year":"2024","journal-title":"J. Agric. Food\nChem."},{"key":"2026090104472290500_cit6","doi-asserted-by":"publisher","DOI":"10.1016\/j.envpol.2023.122581","article-title":"Laccase Lac-W detoxifies aflatoxin\nB1 and degrades five other major\nmycotoxins in the absence of redox mediators","volume":"338","author":"Hao","year":"2023","journal-title":"Environ. 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Macromol."},{"key":"2026090104472290500_cit29","doi-asserted-by":"publisher","DOI":"10.1016\/j.biortech.2024.131983","article-title":"Simultaneous enhancement\nof activity and stability of Bacillus Safensis-derived\nlaccase and its application in lignocellulose saccharification","volume":"418","author":"Yang","year":"2025","journal-title":"Bioresour. Technol."},{"key":"2026090104472290500_cit30","doi-asserted-by":"publisher","DOI":"10.3389\/fpls.2022.832800","article-title":"Identification\nof wheat LACCASEs in response to fusarium\ngraminearum as potential deoxynivalenol trappers","volume":"13","author":"Sun","year":"2022","journal-title":"Front. Plant Sci."},{"issue":"24","key":"2026090104472290500_cit31","doi-asserted-by":"publisher","first-page":"9254","DOI":"10.1073\/pnas.1119460109","article-title":"Flexibility\nof the\nmetal-binding region in apo-cupredoxins","volume":"109","author":"Zaballa","year":"2012","journal-title":"Proc.\nNatl. Acad. Sci. U. S. A."},{"issue":"14","key":"2026090104472290500_cit32","doi-asserted-by":"publisher","first-page":"1502","DOI":"10.1002\/cbic.201800236","article-title":"Structural\ninsight into the allosteric coupling of\nCu1 site and trinuclear Cu cluster in CotA laccase","volume":"19","author":"Xie","year":"2018","journal-title":"ChemBioChem."},{"issue":"9","key":"2026090104472290500_cit33","doi-asserted-by":"publisher","first-page":"4049","DOI":"10.1007\/s00253-018-8875-y","article-title":"Four second-sphere residues of thermus\nthermophilus SG0.5JP17\u201316 laccase tune the catalysis by hydrogen-bonding\nnetworks","volume":"102","author":"Liu","year":"2018","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"2026090104472290500_cit34","doi-asserted-by":"publisher","DOI":"10.3389\/fcell.2022.916114","article-title":"Copper delivery to an endospore coat\nprotein of Bacillus Subtilis","volume":"10","author":"Lee","year":"2022","journal-title":"Front. Cell Dev. 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Macromol."},{"issue":"1","key":"2026090104472290500_cit47","doi-asserted-by":"publisher","first-page":"36","DOI":"10.1186\/s13568-019-0761-1","article-title":"Signal peptide\nreplacement resulted in recombinant homologous expression of laccase\nLcc8 in Coprinopsis Cinerea","volume":"9","author":"Schulze","year":"2019","journal-title":"AMB Express"},{"issue":"12","key":"2026090104472290500_cit48","doi-asserted-by":"publisher","first-page":"6284","DOI":"10.3390\/ijms22126284","article-title":"SRPassing\nCo-Translational Targeting: The role of the signal recognition particle\nin protein targeting and mRNA protection","volume":"22","author":"Kellogg","year":"2021","journal-title":"Int.\nJ. Mol. 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