{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T09:55:57Z","timestamp":1790589357095,"version":"4.1.0"},"reference-count":52,"publisher":"Springer Science and Business Media LLC","issue":"10","license":[{"start":{"date-parts":[[2026,8,12]],"date-time":"2026-08-12T00:00:00Z","timestamp":1786492800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2026,8,12]],"date-time":"2026-08-12T00:00:00Z","timestamp":1786492800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Curr Microbiol"],"published-print":{"date-parts":[[2026,10]]},"DOI":"10.1007\/s00284-026-05091-x","type":"journal-article","created":{"date-parts":[[2026,8,12]],"date-time":"2026-08-12T04:07:44Z","timestamp":1786507664000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Investigation of the Effect of Different Aromatic Compounds and Agro-wastes on Laccase Production by Thermophilic Bacillus Licheniformis SO7 on Gene and Protein Levels"],"prefix":"10.1007","volume":"83","author":[{"given":"Selinay Merve","family":"K\u0131l\u0131\u00e7","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rahime","family":"Altintas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Selma","family":"Saoula","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mustafa \u00d6zkan","family":"Baltaci","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Melda","family":"\u015ei\u015fecio\u011flu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,8,12]]},"reference":[{"key":"5091_CR1","doi-asserted-by":"publisher","first-page":"857","DOI":"10.1007\/s00018-014-1827-5","volume":"72","author":"N Hakulinen","year":"2015","unstructured":"Hakulinen N, Rouvinen J (2015) Three-dimensional structures of laccases. Cell Mol Life Sci 72:857\u2013868. https:\/\/doi.org\/10.1007\/s00018-014-1827-5","journal-title":"Cell Mol Life Sci"},{"issue":"7","key":"5091_CR2","doi-asserted-by":"publisher","first-page":"819","DOI":"10.1080\/07388551.2016.1261081","volume":"37","author":"S Ba","year":"2017","unstructured":"Ba S, Vinoth Kumar V (2017) Recent developments in the use of tyrosinase and laccase in environmental applications. Crit Rev Biotechnol Nov 37(7):819\u2013832. https:\/\/doi.org\/10.1080\/07388551.2016.1261081","journal-title":"Crit Rev Biotechnol Nov"},{"issue":"1","key":"5091_CR3","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1080\/10889869991219163","volume":"3","author":"L Gianfreda","year":"1999","unstructured":"Gianfreda L, Xu F, Bollag JM (1999) Laccases: a useful group of oxidoreductive enzymes. Bioremediat J 3(1):1\u201326. https:\/\/doi.org\/10.1080\/10889869991219163","journal-title":"Bioremediat J"},{"issue":"3","key":"5091_CR4","doi-asserted-by":"publisher","first-page":"318","DOI":"10.1111\/j.1751-7915.2011.00273.x","volume":"5","author":"JR Jeon","year":"2012","unstructured":"Jeon JR, Baldrian P, Murugesan K, Chang YS (2012) Laccase-catalysed oxidations of naturally occurring phenols: from in vivo biosynthetic pathways to green synthetic applications. Microb Biotechnol May 5(3):318\u2013332. https:\/\/doi.org\/10.1111\/j.1751-7915.2011.00273.x","journal-title":"Microb Biotechnol May"},{"issue":"24","key":"5091_CR5","doi-asserted-by":"publisher","first-page":"10327","DOI":"10.1007\/s00253-018-9404-8","volume":"102","author":"A Sharma","year":"2018","unstructured":"Sharma A, Jain KK, Jain A, Kidwai M, Kuhad RC (2018) Bifunctional in vivo role of laccase exploited in multiple biotechnological applications. Appl Microbiol Biotechnol Dec 102(24):10327\u201310343. https:\/\/doi.org\/10.1007\/s00253-018-9404-8","journal-title":"Appl Microbiol Biotechnol Dec"},{"key":"5091_CR6","doi-asserted-by":"publisher","unstructured":"Chaudhary S, Singh A, Varma A, Porwal S (2022) Recent Advancements in Biotechnological Applications of Laccase as a Multifunctional Enzyme. J Pure Appl Microbiol 16(3). https:\/\/doi.org\/10.22207\/JPAM.16.3.72","DOI":"10.22207\/JPAM.16.3.72"},{"issue":"1","key":"5091_CR7","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1007\/s00253-016-7987-5","volume":"101","author":"T Kudanga","year":"2016","unstructured":"Kudanga T, Nemadziva B, Le Roes-Hill M (2016) Laccase catalysis for the synthesis of bioactive compounds. Appl Microbiol Biotechnol 101(1):13\u201333. https:\/\/doi.org\/10.1007\/s00253-016-7987-5","journal-title":"Appl Microbiol Biotechnol"},{"issue":"6","key":"5091_CR8","doi-asserted-by":"publisher","first-page":"1457","DOI":"10.1111\/1751-7915.12422","volume":"10","author":"M Alcalde","year":"2017","unstructured":"Alcalde M, Mate DM (2017) Laccase: a multi-purpose biocatalyst at the forefront of biotechnology. Microb Biotechnol 10(6):1457\u20131467. https:\/\/doi.org\/10.1111\/1751-7915.12422","journal-title":"Microb Biotechnol"},{"issue":"2","key":"5091_CR9","doi-asserted-by":"publisher","first-page":"294","DOI":"10.1080\/07388551.2017.1354353","volume":"38","author":"J Su","year":"2017","unstructured":"Su J, Fu J, Wang Q, Silva C, Cavaco-Paulo A (2017) Laccase: a green catalyst for the biosynthesis of polyphenols. Crit Rev Biotechnol 38(2):294\u2013307. https:\/\/doi.org\/10.1080\/07388551.2017.1354353","journal-title":"Crit Rev Biotechnol"},{"key":"5091_CR10","doi-asserted-by":"publisher","DOI":"10.1007\/s11356-021-13283-0","author":"SK Suman","year":"2021","unstructured":"Suman SK, Malhotra M (2021) Laccase-mediated delignification and detoxification of lignocellulosic biomass: removing obstacles in energy generation. Environ Sci Pollut Res. https:\/\/doi.org\/10.1007\/s11356-021-13283-0","journal-title":"Environ Sci Pollut Res"},{"key":"5091_CR11","doi-asserted-by":"publisher","first-page":"2331","DOI":"10.1016\/j.biortech.2009.10.087","volume":"101","author":"RD Tyagi","year":"2010","unstructured":"Tyagi RD, Majeau JA, Brar SK (2010) Laccases for removal of recalcitrant and emerging pollutants. Bioresour Technol 101:2331\u20132350. https:\/\/doi.org\/10.1016\/j.biortech.2009.10.087","journal-title":"Bioresour Technol"},{"key":"5091_CR12","doi-asserted-by":"publisher","first-page":"101","DOI":"10.1111\/jfbc.12111","volume":"39","author":"W Du","year":"2015","unstructured":"Du W, Sun C, Liang J, Han Y, Yu J, Liang Z (2015) Improvement of laccase production and its characterization by mutagenesis. J Food Biochem 39:101\u2013108. https:\/\/doi.org\/10.1111\/jfbc.12111","journal-title":"J Food Biochem"},{"key":"5091_CR13","doi-asserted-by":"publisher","first-page":"9515","DOI":"10.1007\/s11356-015-4426-6","volume":"22","author":"ZB Guan","year":"2015","unstructured":"Guan ZB, Shui Y, Song CM, Zhang N, Cai YJ, Liao XR (2015) Efficient secretory production of CotA-laccase and its application in the decolorization and detoxification of industrial textile wastewater. Environ Sci Pollut Res 22:9515\u20139523. https:\/\/doi.org\/10.1007\/s11356-015-4426-6","journal-title":"Environ Sci Pollut Res"},{"key":"5091_CR14","doi-asserted-by":"publisher","first-page":"285","DOI":"10.4236\/aim.2014.46035","volume":"4","author":"TAR Fernandes","year":"2014","unstructured":"Fernandes TAR, Silveira WB, Passos FML, Zucchi TD (2014) Laccases from actinobacteria\u2014what we have and what to expect. Post Mikrobiol 4:285\u2013296. https:\/\/doi.org\/10.4236\/aim.2014.46035","journal-title":"Post Mikrobiol"},{"key":"5091_CR15","doi-asserted-by":"publisher","unstructured":"Prins A, Kleinsmidt L, Khan N, Kirby B, Kudanga T, Vollmer J, Pleiss J, Burton S, Le Roes-Hill M (2015) The effect of mutations near the T1 copper site on the biochemical characteristics of the small laccase from Streptomyces coelicolor. Enzym Microb Technol A3(2). https:\/\/doi.org\/10.1016\/j.enzmictec.2014.10.003","DOI":"10.1016\/j.enzmictec.2014.10.003"},{"issue":"1","key":"5091_CR16","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1080\/10826068.2020.1786698","volume":"51","author":"MA El-Bendary","year":"2021","unstructured":"El-Bendary MA, Ezzat SM, Ewais EA, Al-Zalama MA (2021) Optimization of spore laccase production by Bacillus amyloliquefaciens isolated from wastewater and its potential in green biodecolorization of synthetic textile dyes. Prep Biochem Biotechnol 51(1):16\u201327. https:\/\/doi.org\/10.1080\/10826068.2020.1786698","journal-title":"Prep Biochem Biotechnol"},{"issue":"5","key":"5091_CR17","doi-asserted-by":"publisher","first-page":"2211","DOI":"10.1007\/s00203-021-02239-0","volume":"203","author":"L Xue","year":"2021","unstructured":"Xue L, Tang L, Zhao J, Fang Z, Liu H, Qiao J, Zhang G (2021) Bacillus salipaludis sp. nov., isolated from saline-alkaline soil. Arch Microbiol Jul 203(5):2211\u20132217. https:\/\/doi.org\/10.1007\/s00203-021-02239-0","journal-title":"Arch Microbiol Jul"},{"issue":"10","key":"5091_CR18","doi-asserted-by":"publisher","first-page":"954","DOI":"10.1016\/j.fgb.2004.07.002","volume":"41","author":"MC Terr\u00f3n","year":"2004","unstructured":"Terr\u00f3n MC, Gonz\u00e1lez T, Carbajo JM, Yag\u00fce S, Arana-Cuenca A, T\u00e9llez A, Gonz\u00e1lez AE (2004) Structural close-related aromatic compounds have different effects on laccase activity and on lcc gene expression in the ligninolytic fungus Trametes sp. I-62. Fungal Genet Biol 41(10):954\u2013962. https:\/\/doi.org\/10.1016\/j.fgb.2004.07.002","journal-title":"Fungal Genet Biol"},{"key":"5091_CR19","doi-asserted-by":"publisher","first-page":"1558","DOI":"10.3389\/fmicb.2015.01558","volume":"6","author":"J Yang","year":"2016","unstructured":"Yang J, Wang G, Ng TB, Lin J, Ye X (2016) Laccase production and differential transcription of laccase genes in Cerrena sp. in response to metal ions, aromatic compounds, and nutrients. Front Microbiol 6:1558. https:\/\/doi.org\/10.3389\/fmicb.2015.01558","journal-title":"Front Microbiol"},{"key":"5091_CR20","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.enzmictec.2012.10.003","volume":"52","author":"G Janusz","year":"2013","unstructured":"Janusz G, Kucharzyk KH, Pawlik A, Staszczak M, Paszczynski AJ (2013) Fungal laccase, manganese peroxidase and lignin peroxidase: geneexpressionandregulation. EnzymeMicrob Technol 52:1\u201312. https:\/\/doi.org\/10.1016\/j.enzmictec.2012.10.003","journal-title":"EnzymeMicrob Technol"},{"key":"5091_CR21","doi-asserted-by":"publisher","first-page":"104","DOI":"10.2174\/138920211795564331","volume":"12","author":"A Piscitelli","year":"2011","unstructured":"Piscitelli A, Giardina P, Lettera V, Pezzella C, Sannia G, Faraco V (2011) Induction and Transcriptional Regulation of Laccases in Fungi. Curr Genom 12:104\u2013122. https:\/\/doi.org\/10.2174\/138920211795564331","journal-title":"Curr Genom"},{"issue":"4","key":"5091_CR22","doi-asserted-by":"publisher","first-page":"1015","DOI":"10.1002\/btpr.2482","volume":"33","author":"B Bertrand","year":"2017","unstructured":"Bertrand B, Mart\u00ednez-Morales F, Trejo-Hern\u00e1ndez MR (2017) Upgrading Laccase Production and Biochemical Properties: Strategies and Challenges. Biotechnol Prog Jul 33(4):1015\u20131034. https:\/\/doi.org\/10.1002\/btpr.2482","journal-title":"Biotechnol Prog Jul"},{"key":"5091_CR23","unstructured":"\u00d6lmez S (2017) Isolation and identification of thermophilic bacteria isolated from Nev\u015fehir Kozakl\u0131 hot springs, purification and characterization of \u03b1-amylase enzyme from Bacillus licheniformis SO7, Atat\u00fcrk University, Institute of Science, Master\u2019s Thesis, Erzurum"},{"issue":"3","key":"5091_CR24","doi-asserted-by":"publisher","first-page":"294","DOI":"10.1002\/jobm.201500230","volume":"56","author":"AN Yadav","year":"2016","unstructured":"Yadav AN, Sachan SG, Verma P, Kaushik R, Saxena AK (2016) Cold active hydrolytic enzymes production by psychrotrophic Bacilli isolated from three sub-glacial lakes of NW Indian Himalayas. J Basic Microbiol Mar 56(3):294\u2013307 PMID: 26933936. https:\/\/doi.org\/10.1002\/jobm.201500230","journal-title":"J Basic Microbiol Mar"},{"issue":"2","key":"5091_CR25","doi-asserted-by":"publisher","first-page":"715","DOI":"10.1128\/jb.112.2.715-725.1972","volume":"112","author":"VL Clark","year":"1972","unstructured":"Clark VL, Peterson DE, Bernlohr RW (1972) Changes in free amino acid production and intracellular amino acid pools of Bacillus licheniformisas a function of culture age and growth media. J Bacteriol Nov 112(2):715\u2013725. https:\/\/doi.org\/10.1128\/jb.112.2.715-725.1972","journal-title":"J Bacteriol Nov"},{"issue":"9","key":"5091_CR26","doi-asserted-by":"publisher","first-page":"5926","DOI":"10.1166\/jnn.2010.2614","volume":"10","author":"G Kedia","year":"2010","unstructured":"Kedia G, Hilll D, Hill R, Radecka I (2010) Production of poly-gamma-glutamic acid by Bacillus subtilis and Bacillus licheniformis with different growth media. J Nanosci Nanotechnol Sep 10(9):5926\u20135934. https:\/\/doi.org\/10.1166\/jnn.2010.2614","journal-title":"J Nanosci Nanotechnol Sep"},{"issue":"1","key":"5091_CR27","doi-asserted-by":"publisher","first-page":"70","DOI":"10.1128\/jb.99.1.70-77.1969","volume":"99","author":"J Spizizen","year":"1969","unstructured":"Spizizen J, Prestidge L (1969) Conditions for competence in the Bacillus licheniformis transformation system. J Bacteriol Jul 99(1):70\u2013. https:\/\/doi.org\/10.1128\/jb.99.1.70-77.1969. 7","journal-title":"J Bacteriol Jul"},{"key":"5091_CR28","unstructured":"\u00d6ztat K (2023) Optimization studies on laccase activities of bacteria isolated from wastewater treatment and sludge of paper and textile industry factories, Osmangazi University, Institute of Science, Master\u2019s Thesis, Eski\u015fehir"},{"key":"5091_CR29","doi-asserted-by":"publisher","first-page":"e00566","DOI":"10.1016\/j.btre.2020.e00566","volume":"20","author":"TC Ezike","year":"2020","unstructured":"Ezike TC, Ezugwu AL, Udeh JO, Eze SOO, Chilaka FC (2020) Purification and characterization of new laccase from Trametes polyzona WRF03. Biotechnol Rep (Amst). Nov 20:28:e00566. https:\/\/doi.org\/10.1016\/j.btre.2020.e00566","journal-title":"Nov"},{"issue":"1","key":"5091_CR30","doi-asserted-by":"publisher","first-page":"265","DOI":"10.1016\/S0021-9258(19)52451-6","volume":"193","author":"OH Lowry","year":"1951","unstructured":"Lowry OH, Rosebrough Nj, Farr AI, Randall Rj (1951) Protein measurement with the Fol\u015fn phenol resmen. J Biol Chem Nov 193(1):265\u2013275. https:\/\/doi.org\/10.1016\/S0021-9258(19)52451-6","journal-title":"J Biol Chem Nov"},{"key":"5091_CR31","doi-asserted-by":"publisher","first-page":"680","DOI":"10.1038\/227680a0","volume":"227","author":"DK Laemmli","year":"1970","unstructured":"Laemmli DK (1970) Cleavage of structural proteins during in assembly of the head of Bacteriophage T4. Nature 227:680. https:\/\/doi.org\/10.1038\/227680a0","journal-title":"Nature"},{"key":"5091_CR32","doi-asserted-by":"publisher","DOI":"10.1186\/s13068-019-1606-5","author":"R Morya","year":"2019","unstructured":"Morya R, Kumar M, Singh SS, Thakur IS (2019) Genomic analysis of Burkholderia sp. ISTR5 for biofunneling of lignin-derived compounds. Biotechnol Biofuels. https:\/\/doi.org\/10.1186\/s13068-019-1606-5","journal-title":"Biotechnol Biofuels"},{"key":"5091_CR33","doi-asserted-by":"publisher","unstructured":"Kocyigit A, Pazarbasi MB, Yasa I, Ozdemir G, Karaboz I (2012) Production of laccase from Trametes trogii TEM H2: a newly isolated white-rot fungus by air sampling. J Basic Microbiol. Dec;52(6):661-9. https:\/\/doi.org\/10.1002\/jobm.201100341. Epub 2012 Feb 23. PMID: 22359264","DOI":"10.1002\/jobm.201100341"},{"key":"5091_CR34","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/s13568-014-0092-1","volume":"5","author":"GS Kaira","year":"2015","unstructured":"Kaira GS, Dhakar K, Pandey A (2015) A psychrotolerant strain of Serratia marcescens (MTCC 4822) produces laccase at wide temperature and pH range. Amb Express 5:1\u20138. https:\/\/doi.org\/10.1186\/s13568-014-0092-1","journal-title":"Amb Express"},{"key":"5091_CR35","doi-asserted-by":"publisher","first-page":"1429","DOI":"10.1007\/s10529-021-03131-z","volume":"43","author":"A Gogotya","year":"2021","unstructured":"Gogotya A, Nnolim NE, Digban TO, Okoh AI, Nwodo UU (2021) Characterization of a thermostable and solvent-tolerant laccase produced by Streptomyces sp. LAO Biotechnol Lett 43:1429\u20131442. https:\/\/doi.org\/10.1007\/s10529-021-03131-z","journal-title":"LAO Biotechnol Lett"},{"issue":"6","key":"5091_CR36","doi-asserted-by":"publisher","first-page":"993","DOI":"10.1007\/s00792-017-0958-7","volume":"21","author":"R Rezaie","year":"2017","unstructured":"Rezaie R, Rezaei S, Jafari N, Forootanfar H, Khoshayand MR, Faramarzi MA (2017) Delignification and detoxification of peanut shell bio-waste using an extremely halophilic laccase from an Aquisalibacillus elongatus isolate. Extremophiles Nov 21(6):993\u20131004. https:\/\/doi.org\/10.1007\/s00792-017-0958-7","journal-title":"Extremophiles Nov"},{"key":"5091_CR37","doi-asserted-by":"publisher","first-page":"127416","DOI":"10.1016\/j.micres.2023.127416","volume":"274","author":"I Mutanda","year":"2023","unstructured":"Mutanda I, Zahoor, Sethupathy S, Xu Q, Zhu B, Shah SWA, Zhuang Z, Zhu D (2023) Optimization of heterologous production of Bacillus ligniniphilus L1 laccase in Escherichia coli through statistical design of experiments. Microbiol Res Sep 274:127416. https:\/\/doi.org\/10.1016\/j.micres.2023.127416","journal-title":"Microbiol Res Sep"},{"key":"5091_CR38","doi-asserted-by":"publisher","unstructured":"Kumar V, Chandra R (2018) Characterisation of manganese peroxidase and laccase producing bacteria capable for degradation of sucrose glutamic acid-Maillard reaction products at different nutritional and environmental conditions. World J Microbiol Biotechnol. Feb 2;34(2):32. https:\/\/doi.org\/10.1007\/s11274-018-2416-9","DOI":"10.1007\/s11274-018-2416-9"},{"issue":"14","key":"5091_CR39","doi-asserted-by":"publisher","first-page":"9741","DOI":"10.1021\/acsomega.1c00370","volume":"6","author":"YP Jiang","year":"2021","unstructured":"Jiang YP, Cai JL, Pei JJ, Li Q, Zhao LG (2021) Cloning, overexpression, and characterization of a thermostable, organic solvent-tolerant laccase from Bacillus pumilus ARA and its application to dye decolorization. ACS omega 6(14):9741\u20139749. https:\/\/doi.org\/10.1021\/acsomega.1c00370","journal-title":"ACS omega"},{"key":"5091_CR40","doi-asserted-by":"publisher","unstructured":"Kumar S, Jain KK, Bhardwaj KN, Chakraborty S, Kuhad RC (2015) Multiple Genes in a Single Host: Cost-Effective Production of Bacterial Laccase (cotA), Pectate Lyase (pel), and Endoxylanase (xyl) by Simultaneous Expression and Cloning in Single Vector in E. coli. PLoS One. Dec 7;10(12):e0144379. https:\/\/doi.org\/10.1371\/journal.pone.0144379","DOI":"10.1371\/journal.pone.0144379"},{"issue":"3","key":"5091_CR41","doi-asserted-by":"publisher","first-page":"403","DOI":"10.1007\/s00449-019-02236-0","volume":"43","author":"J Wang","year":"2020","unstructured":"Wang J, Yu S, Li X, Feng F, Lu L (2020) High-level expression of Bacillus amyloliquefaciens laccase and construction of its chimeric variant with improved stability by domain substitution. Bioprocess Biosyst Eng Mar 43(3):403\u2013411. https:\/\/doi.org\/10.1007\/s00449-019-02236-0","journal-title":"Bioprocess Biosyst Eng Mar"},{"issue":"2","key":"5091_CR42","doi-asserted-by":"publisher","first-page":"175","DOI":"10.1007\/s13205-014-0207-z","volume":"5","author":"S Sondhi","year":"2015","unstructured":"Sondhi S, Sharma P, George N, Chauhan PS, Puri N, Gupta N (2015) An extracellular thermo-alkali-stable laccase from Bacillus tequilensis SN4, with a potential to biobleach softwood pulp. 3 Biotech Apr 5(2):175\u2013185. https:\/\/doi.org\/10.1007\/s13205-014-0207-z","journal-title":"3 Biotech Apr"},{"key":"5091_CR43","doi-asserted-by":"publisher","first-page":"878360","DOI":"10.3389\/fmicb.2022.878360","volume":"13","author":"NS Ali","year":"2022","unstructured":"Ali NS, Huang F, Qin W, Yang TC (2022) Identification and Characterization of a New Serratia proteamaculans Strain That Naturally Produces Significant Amount of Extracellular Laccase. Front Microbiol 13:878360. https:\/\/doi.org\/10.3389\/fmicb.2022.878360","journal-title":"Front Microbiol"},{"issue":"1","key":"5091_CR44","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1007\/s13205-016-0425-7","volume":"6","author":"M Neifar","year":"2016","unstructured":"Neifar M, Chouchane H, Mahjoubi M, Jaouani A, Cherif A (2016) Pseudomonas extremorientalis BU118: a new salt-tolerant laccase-secreting bacterium with biotechnological potential in textile azo dye decolourization. 3 Biotech 6(1):107. https:\/\/doi.org\/10.1007\/s13205-016-0425-7","journal-title":"3 Biotech"},{"issue":"5","key":"5091_CR45","doi-asserted-by":"publisher","first-page":"e96951","DOI":"10.1371\/journal.pone.0096951","volume":"9","author":"S Sondhi","year":"2014","unstructured":"Sondhi S, Sharma P, Saini S, Puri N, Gupta N (2014) Purification and characterization of an extracellular, thermo-alkali-stable, metal tolerant laccase from Bacillus tequilensis SN4. PLoS ONE 9(5):e96951. https:\/\/doi.org\/10.1371\/journal.pone.0096951","journal-title":"PLoS ONE"},{"key":"5091_CR46","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/s40201-016-0244-0","volume":"20","author":"D Daassi","year":"2016","unstructured":"Daassi D, Zouari-Mechichi H, Frikha F, Rodriguez-Couto S, Nasri M, Mechichi T (2016) Sawdust waste as a low-cost support-substrate for laccase production and adsorbent for azo dyes decoloration. J Environ Health Sci Eng Jan 20:14:1. https:\/\/doi.org\/10.1186\/s40201-016-0244-0","journal-title":"J Environ Health Sci Eng Jan"},{"issue":"22","key":"5091_CR47","doi-asserted-by":"publisher","first-page":"4441","DOI":"10.1080\/09593330.2023.2253503","volume":"45","author":"CE Edoamodu","year":"2024","unstructured":"Edoamodu CE, Nwodo UU (2024) Optimization and physicochemical characterization of a termo-alkali stable laccase production by wastewater associated Bacillus sp. NU2. Environ Technol Sep 45(22):4441\u20134456 PMID: 37641161. https:\/\/doi.org\/10.1080\/09593330.2023.2253503","journal-title":"Environ Technol Sep"},{"key":"5091_CR48","doi-asserted-by":"publisher","unstructured":"Palazzalo MA, Postemsky PD, Kurina-Sanz M (2019) From argo-waste to tool: biotechnological characterization and application of Ganoderma lucidium E47 laccase in dye decolorization. 3 Biotech. 9(6):213. https:\/\/doi.org\/10.1007\/s13205-019-1744-2","DOI":"10.1007\/s13205-019-1744-2"},{"issue":"3","key":"5091_CR49","doi-asserted-by":"publisher","first-page":"507","DOI":"10.1007\/s00449-019-02245-z","volume":"43","author":"VE Pinheiro","year":"2020","unstructured":"Pinheiro VE, Michelin M, Vici AC, de Almeida PZ, de Teixeria ML (2020) Trametes versicolor laccase production using agricultural wastes: a comparative study in erlenmeyer flasks, bioreactor and tray. Bioprocess Biosyst Eng Mar 43(3):507\u2013514. https:\/\/doi.org\/10.1007\/s00449-019-02245-z","journal-title":"Bioprocess Biosyst Eng Mar"},{"key":"5091_CR50","doi-asserted-by":"publisher","unstructured":"Thamvithayakorn P, Phosri C, Pisutpaisal N, Krajangsang S, Whalley AJS, Suwannasai N (2019) Utilization of oil palm decanter cake for valuable laccase and manganase poroxidase enzyme production from a Nobel white-rot fungus, Pseudolagarobasidium sp. PP17-33. 3 Biotech. 9(11):417. https:\/\/doi.org\/10.1007\/s13205-019-1945-8","DOI":"10.1007\/s13205-019-1945-8"},{"issue":"1","key":"5091_CR51","doi-asserted-by":"publisher","first-page":"16","DOI":"10.3923\/pjbs.2025.16.26","volume":"28","author":"T Yuliana","year":"2025","unstructured":"Yuliana T, Fauziah E, Martha H, Safirti R, Krama A (2025) Laccase characterization from Ganodermalucidum growth in pineapple and coffee waste substrates under solid fermentation. Pak J Biol Sci Jan 28(1):16\u201326. https:\/\/doi.org\/10.3923\/pjbs.2025.16.26","journal-title":"Pak J Biol Sci Jan"},{"key":"5091_CR52","doi-asserted-by":"publisher","first-page":"747","DOI":"10.1007\/s00253-018-9468-5","volume":"103","author":"Y Ma","year":"2019","unstructured":"Ma Y, Li L, Tian H, Lu M, Megharaj M, He W (2019) Transcriptional analysis of the laccase-like gene from Burkholderia cepacia BNS and expression in Escherichia coli. Appl Microbiol Biotechnol 103:747\u2013760. https:\/\/doi.org\/10.1007\/s00253-018-9468-5","journal-title":"Appl Microbiol Biotechnol"}],"container-title":["Current Microbiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00284-026-05091-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s00284-026-05091-x","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00284-026-05091-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T09:06:09Z","timestamp":1790586369000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s00284-026-05091-x"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,12]]},"references-count":52,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2026,10]]}},"alternative-id":["5091"],"URL":"https:\/\/doi.org\/10.1007\/s00284-026-05091-x","relation":{},"ISSN":["0343-8651","1432-0991"],"issn-type":[{"value":"0343-8651","type":"print"},{"value":"1432-0991","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,12]]},"assertion":[{"value":"3 November 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"29 July 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"12 August 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","label":"Competing interests","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Ethical approval is not applicable.","order":2,"name":"Ethics","label":"Ethics approval","group":{"name":"EthicsHeading","label":"Declarations"}}],"article-number":"510"}}