{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,27]],"date-time":"2026-04-27T11:16:40Z","timestamp":1777288600137,"version":"3.51.4"},"reference-count":69,"publisher":"MDPI AG","issue":"17","license":[{"start":{"date-parts":[[2021,9,4]],"date-time":"2021-09-04T00:00:00Z","timestamp":1630713600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Cold-adapted enzymes are useful tools in the organic syntheses conducted in mixed aqueous-organic or non-aqueous solvents due to their molecular flexibility that stabilizes the proteins in low water activity environments. A novel psychrophilic laccase gene from Kabatiella bupleuri, G3 IBMiP, was spliced by Overlap-Extension PCR (OE-PCR) and expressed in Pichia pastoris. Purified recombinant KbLcc1 laccase has an optimal temperature of 30 \u00b0C and pH of 3.5, 5.5, 6.0, and 7.0 in the reaction with 2,2\u2032-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), guaiacol, sinapic acid, and syringaldazine, respectively. Moreover, laccase KbLcc1 is highly thermolabile, as it loses 40% of activity after 30 min at 40 \u00b0C and is inactivated at 50 \u00b0C after the same period of incubation. The new enzyme remained active with 1 mM of Ni2+, Cu2+, Mn2+, and Zn2+ and with 2 mM of Co2+, Ca2+, and Mg2+, but Fe2+ greatly inhibited the laccase activity. Moreover, 1% ethanol had no impact on KbLcc1, although acetone and ethyl acetate decreased the laccase activity. The presence of hexane (40%, v\/v) caused a 58% increase in activity. Laccase KbLcc1 could be applied in the decolorization of synthetic dyes and in the biotransformation of ferulic acid to vanillin. After 5 days of reaction at 20 \u00b0C, pH 3.5, with 1 mM ABTS as a mediator, the vanillin concentration was 21.9 mg\/L and the molar yield of transformation reached 14.39%.<\/jats:p>","DOI":"10.3390\/ijms22179593","type":"journal-article","created":{"date-parts":[[2021,9,6]],"date-time":"2021-09-06T13:15:56Z","timestamp":1630934156000},"page":"9593","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":22,"title":["Novel Cold-Adapted Recombinant Laccase KbLcc1 from Kabatiella bupleuri G3 IBMiP as a Green Catalyst in Biotransformation"],"prefix":"10.3390","volume":"22","author":[{"given":"Katarzyna M.","family":"Wi\u015bniewska","sequence":"first","affiliation":[{"name":"Institute of Molecular and Industrial Biotechnology, Lodz University of Technology, Stefanowskiego 2\/22, 90-537 \u0141\u00f3d\u017a, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Aleksandra","family":"Twarda-Clapa","sequence":"additional","affiliation":[{"name":"Institute of Molecular and Industrial Biotechnology, Lodz University of Technology, Stefanowskiego 2\/22, 90-537 \u0141\u00f3d\u017a, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Aneta M.","family":"Bia\u0142kowska","sequence":"additional","affiliation":[{"name":"Institute of Molecular and Industrial Biotechnology, Lodz University of Technology, Stefanowskiego 2\/22, 90-537 \u0141\u00f3d\u017a, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2021,9,4]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"6119","DOI":"10.1046\/j.1432-1033.2002.03324.x","article-title":"Characterization of low redox potential laccase from the basidiomycete C30","volume":"269","author":"Klonowska","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"ref_2","first-page":"67","article-title":"Fungal laccases","volume":"37","year":"2013","journal-title":"Fungal Biol. Rev."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.biotechadv.2014.12.007","article-title":"Laccase engineering: From rational design to directed evolution","volume":"33","author":"Mate","year":"2015","journal-title":"Biotechnol. Adv."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Pourmir, A., and Johannes, T.W. (2012). Directed evolution: Selection of the host organism. Comput. Struct. Biotechnol. J., 2.","DOI":"10.5936\/csbj.201209012"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"252","DOI":"10.4161\/bbug.1.4.11438","article-title":"Heterologous laccase production and its role in industrial applications","volume":"1","author":"Piscitelli","year":"2010","journal-title":"Bioeng. Bugs"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/S1381-1177(01)00062-5","article-title":"Biobleaching of pulp with dioxygen in laccase-mediator system\u2014Effect of variables on the reaction kinetics","volume":"16","author":"Balakshin","year":"2001","journal-title":"J. Mol. Catal. B Enzym."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/j.molcatb.2006.12.004","article-title":"Phenols removal in musts: Strategy for wine stabilization by laccase","volume":"45","author":"Minussi","year":"2007","journal-title":"J. Mol. Catal. B Enzym."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1038\/nbt982","article-title":"Ex planta phytoremediation of trichlorophenol and phenolic allelo chemicals via an engineered secretory laccase","volume":"22","author":"Wang","year":"2004","journal-title":"Nat. Biotechnol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.jclepro.2015.03.047","article-title":"Removal of micropollutants by fungal laccases in model solution and municipal wastewater: Evaluation of estrogenic activity and ecotoxicity","volume":"100","author":"Spina","year":"2015","journal-title":"J. Clean Prod."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.ecoenv.2018.05.078","article-title":"Asparagus densiflorus in a vertical subsurface flow phytoreactor for treatment of real textile effluent: A lab to land approach for in situ soil remediation","volume":"161","author":"Watharkar","year":"2018","journal-title":"Ecotoxicol. Environ. Saf."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Liu, H., Cheng, Y., Du, B., Tong, C., Liang, S., Han, S., Zheng, S., and Lin, Y. (2015). Overexpression of a novel thermostable and chloride-tolerant laccase from Thermus thermophilus SG0.5 JP17-16 in Pichia pastoris and its application in synthetic dye decolorization. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0119833"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"6397","DOI":"10.1021\/acs.jafc.6b02187","article-title":"Rice (Oryza sativa) laccases involved in modification and detoxification of herbicides atrazine and izoproturon residues in plants","volume":"64","author":"Huang","year":"2016","journal-title":"J. Agric. Food Chem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.chemosphere.2016.01.019","article-title":"Oxidation of polycyclic aromatic hydrocarbons using Bacillus CotA with high laccase activity and copper independence","volume":"148","author":"Zheng","year":"2016","journal-title":"Chemosphere"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/j.scitotenv.2017.12.127","article-title":"Characterization of electron beam irradiation-immobilised laccase for application in wastewater treatment","volume":"624","author":"Jahangiri","year":"2018","journal-title":"Sci. Total Environ."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"7551","DOI":"10.1016\/S0040-4039(01)01463-0","article-title":"An oxidation of alcohols by oxygen with the enzyme laccase and mediation by TEMPO","volume":"42","author":"Fabbrini","year":"2001","journal-title":"Tetrahedron Lett."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1016\/j.tet.2003.10.117","article-title":"Biotransformation of resveratrol: Synthesis of trans-dehydrodimers catalyzed by laccases from Myceliophtora thermophyla and from Trametes pubescens","volume":"60","author":"Nicotra","year":"2004","journal-title":"Tetrahedron"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1002\/mabi.200300038","article-title":"Laccase-catalyzed synthesis and antioxidant property of poly(catechin)","volume":"3","author":"Kurisawa","year":"2003","journal-title":"Macromol. Biosci."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1039\/b312311a","article-title":"Oxidative coupling of epigallocatechin gallate amplifies antioxidant activity and inhibits xanthine oxidase activity","volume":"3","author":"Kurisawa","year":"2004","journal-title":"Chem. Commun."},{"key":"ref_19","first-page":"193","article-title":"The chemistry of hair colorants","volume":"116","author":"Anderson","year":"2000","journal-title":"J. Soc. Dyers Colour."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1002\/elsc.200700061","article-title":"Biological coloration of flax fabrics with flavonoids using laccase from Trametes hirsute","volume":"8","author":"Kim","year":"2008","journal-title":"Eng. Life Sci."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1016\/j.foodres.2005.02.019","article-title":"Phenolic colorants obtained by enzymatic synthesis using a fungal laccase in a hydro-organic biphasic system","volume":"38","author":"Mustafa","year":"2015","journal-title":"Food Res. Int."},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Schwab, W., Lange, B., and W\u00fcst, M. (2018). Vanilla: The most popular flavour. Biotechnology of Natural Products, Springer.","DOI":"10.1007\/978-3-319-67903-7"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1016\/j.jclepro.2018.02.043","article-title":"Cleaner production of vanillin through biotransformation of ferulic acid esters from agro residue by Streptomyces sannanensis","volume":"182","author":"Chattopadhyay","year":"2018","journal-title":"J. Clean Prod."},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Tang, P.L., and Hassan, O. (2020). Bioconversion of ferulic acid attained from pineapple peels and pineapple crown leaves into vanilic acid and vanillin by Aspergillus niger I-1472. BMC Chem., 14.","DOI":"10.1186\/s13065-020-0663-y"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1007\/s10068-017-0019-0","article-title":"Optimizing bioconversion of ferulic acid to vanillin by Bacillus subtilis in the stirred packed reactor using Box-Behnken design and desirability function","volume":"26","author":"Chen","year":"2017","journal-title":"Food Sci. Biotechnol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1677","DOI":"10.1007\/s00253-015-7005-3","article-title":"Ferulic acid transformation into the main vanilla aroma compounds by Amycolatopsis sp. ATCC 39116","volume":"100","author":"Agrasar","year":"2016","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/0168-1656(94)90003-5","article-title":"Vanillin as a product of ferulic acid biotransformation by the white-rot fungus Pycnoporus cinnabarinus I-937: Identification of metabolic pathways","volume":"37","author":"Falconnier","year":"1994","journal-title":"J. Biotechnol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/j.nbt.2015.03.002","article-title":"High-yield production of vanillin from ferulic acid by a coenzyme-independent decarboxylase\/oxygenase two-stage process","volume":"32","author":"Furuya","year":"2015","journal-title":"N. Biotechnol."},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Wi\u015bniewska, K.M., Twarda-Clapa, A., and Bia\u0142kowska, A.M. (2021). Screening of novel laccase producers\u2014Isolation and characterization of cold-adapted laccase from Kabatiella bupleuri G3 capable of synthetic dye decolorization. Biomolecules, 11.","DOI":"10.3390\/biom11060828"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1038\/nprot.2007.132","article-title":"Gene splicing and mutagenesis by PCR-driven overlap extension","volume":"2","author":"Heckman","year":"2007","journal-title":"Nat. Protoc."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Viswanath, B., Rajesh, B., Janardhan, A., Kumar, A.P., and Narasimha, G. (2014). Fungal laccases and their application in bioremediation. Enzyme Res., 2014.","DOI":"10.1155\/2014\/163242"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"278","DOI":"10.3906\/biy-1605-51","article-title":"Heterologus expression and characterization of a high redox potential laccase from Coriolopsis polyzona MUCL 38443","volume":"41","author":"Pinar","year":"2017","journal-title":"Turk. J. Biol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1927","DOI":"10.1007\/s11033-012-2249-9","article-title":"Heterologous expression and characterization of a novel laccase isoenzyme with dyes decolorization potential from Coprinus comatus","volume":"40","author":"Bao","year":"2013","journal-title":"Mol. Biol. Rep."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1134\/S0003683814020124","article-title":"Overexpression and characterization of laccase from Trametes versicolor in Pichia pastoris","volume":"50","author":"Li","year":"2014","journal-title":"Appl. Biochem. Microbiol."},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Wang, B., Yan, Y., Tian, Y., Zhao, W., Li, Z., Gao, J., Peng, R., and Yao, Q. (2016). Heterologous expression and characterization of a laccase from Colletotrichum lagenarium and decolourisation of different synthetic dyes. World J. Microbiol. Biotechnol., 32.","DOI":"10.1007\/s11274-015-1999-7"},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Arregui, L., Ayala, M., Gomez-Gil, X., Gutierrez-Soto, G., Hernandez-Luna, C.E., de los Santos, M.H., Levin, L., Rojo-Dominguez, A., Romero-Martinez, D., and Saparrat, M.C. (2019). Laccase: Structure, function, and potential application in water bioremediation. Microb. Cell Factories, 18.","DOI":"10.1186\/s12934-019-1248-0"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1016\/j.sjbs.2013.04.001","article-title":"Characterization and kinetic properties of the purified Trematosphaeria mangrovei laccase enzyme","volume":"20","author":"Atalla","year":"2013","journal-title":"Saudi J. Biol. Sci."},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Maestre-Reyna, M., Liu, W.C., Jeng, W.Y., Lee, C.C., Hsu, C.A., Wen, T.N., Wang, A.H., and Shyur, L.F. (2015). Structural and functional roles of glycosylation in fungal laccase from Lentinus sp.. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0120601"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.enzmictec.2013.03.015","article-title":"Laccases from Aureobasidium pullulans","volume":"53","author":"Rich","year":"2013","journal-title":"Enzyme Microb. Technol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1007\/s10126-018-9860-2","article-title":"Production, gene cloning and overexpression of a laccase in the marine-derived yeast Aureobasidium melanogenum strain 11-1 and characterization of the recombinant laccase","volume":"21","author":"Aung","year":"2019","journal-title":"Mar. Biotechnol."},{"key":"ref_41","first-page":"41","article-title":"Laccase production by diverse phylogenetic clades of Aureobasidium pullulans","volume":"1","author":"Rich","year":"2011","journal-title":"RJAS"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1744","DOI":"10.1016\/j.ijbiomac.2018.09.175","article-title":"Purification and characterization of a fungal laccase from the ascomycete Thielavia sp. and its role in the decolorization of a recalcitrant dye","volume":"120","author":"Barriuso","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1007\/s10529-017-2461-8","article-title":"Characterization of a mildly alkalophilic and thermostable recombinant Thermus thermiphilus laccase with applications in decolourization of dyes","volume":"40","author":"Kumari","year":"2018","journal-title":"Biotechnol. Lett."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1111\/j.1574-4976.2005.00010.x","article-title":"Fungal laccases\u2014Occurrence and properties","volume":"30","author":"Baldrian","year":"2006","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1007\/s00253-002-1012-x","article-title":"Purification and characterization of a novel laccase from the ascomycete Melanocarpus albomyces","volume":"59","author":"Kiiskinen","year":"2002","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1046\/j.1432-1033.2003.03930.x","article-title":"Biochemical and molecular characterization of a laccase from the edible straw mushroom, Volvariella volvacea","volume":"271","author":"Chen","year":"2004","journal-title":"Eur. J. Biochem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/j.procbio.2012.12.011","article-title":"Purification and characterization of a new laccase from Shiraia sp. SUPER-H168","volume":"48","author":"Yang","year":"2013","journal-title":"Process Biochem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1080\/10826068.2011.577882","article-title":"Characterization of laccase activity produced by Cryptococcus albidus","volume":"42","author":"Singhal","year":"2012","journal-title":"Prep. Biochem. Biotechnol."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Yang, Q., Zhang, M., Zhang, M., Wang, C., Liu, Y., Fan, X., and Li, H. (2018). Characterization of a novel, cold-adapted and thermostable laccase-like enzyme with high tolerance for organic solvents and salt and potent dye decolorization ability, derived from a marine metagenomic library. Front. Microbiol., 9.","DOI":"10.3389\/fmicb.2018.02998"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1111\/j.1751-7915.2011.00258.x","article-title":"Biotechnological uses of enzymes from psychrophiles","volume":"4","author":"Cavicchioli","year":"2011","journal-title":"Microb. Biotechnol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1002\/jobm.201200808","article-title":"Molecular cloning of a laccase gene from Ganoderma lucidum and heterologous expression in Pichia pastoris","volume":"54","author":"You","year":"2014","journal-title":"J. Basic Microbiol."},{"key":"ref_52","first-page":"451","article-title":"Molecular characterization of a novel thermostable laccase PLLCC2 from the brown rot fungus Postia placenta MAD-698-R. Electron","volume":"18","author":"An","year":"2015","journal-title":"J. Biotechnol."},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Mandic, M., Djokic, L., Nikolaivits, E., Prodanovic, R., O\u2019Connor, K., Jeremic, S., Topakas, E., and Nikodinovic-Runic, J. (2019). Identification and characterization of new laccase biocatalysts from Pseudomonas species suitable for degradation of synthetic textile dyes. Catalysts, 9.","DOI":"10.3390\/catal9070629"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1134\/S0003683815040080","article-title":"Production, purification and characterization of novel laccase produced by Schizophyllum commune NI-07 with potential for delignification of crop residues","volume":"51","author":"Kumar","year":"2015","journal-title":"Appl. Biochem. Microbiol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/j.molcatb.2011.07.014","article-title":"Purification and characterization of a novel trimeric and thermotolerant laccase produced from the ascomycete Scytalidium thermophilum strain","volume":"73","author":"Younes","year":"2011","journal-title":"J. Mol. Catal. B Enzym."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1016\/j.ijbiomac.2020.12.082","article-title":"Purification and characterization of a novel white highly thermo stable laccase from a novel Bacillus sp. MSK-01 having potential to be used as anticancer agent","volume":"170","author":"Sondhi","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.molcatb.2014.06.006","article-title":"Purification and characterization of two thermostable laccases from Pycnoporus sanguineus and potential role in degradation of endocrine disrupting chemicals","volume":"108","author":"Junghanns","year":"2014","journal-title":"J. Mol. Catal. B Enzym."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/j.ijbiomac.2020.09.137","article-title":"Suitability of organic solvent and cholinium based ionic liquid activated novel lignolytic enzymes of H. aswanensis for enhanced Kalson lignin degradation","volume":"165","author":"Chauhan","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_59","doi-asserted-by":"crossref","unstructured":"Ezike, T.C., Ezugwu, A.L., Udeh, J.O., Eze, S.O., and Chilaka, F.C. (2020). Purification and characterisation of new laccase from Trametes polyzona WRF03. Biotechnol. Rep., 28.","DOI":"10.1016\/j.btre.2020.e00566"},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Jafari, M., Mojtabavi, S., Faramarzi, M.A., Mehrnejad, F., Soleimani, M., and Mirjani, R. (2020). Molecular level insight into stability, activity and structure of laccase in aqueous ionic liquid and organic solvents: An experimental and computational research. J. Mol. Liq., 317.","DOI":"10.1016\/j.molliq.2020.113925"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1007\/s11274-013-1440-z","article-title":"Production of the Phanerochaete flavido-alba laccase in Aspergillus niger for synthetic dyes decolorization and biotransformation","volume":"30","author":"Benghazi","year":"2014","journal-title":"World J. Microbiol. Biotechnol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1232","DOI":"10.1007\/s00253-006-0767-x","article-title":"Purification and characterization of laccase from Pycnoporus sanguineus and decolorization of an anthraquinone dye by the enzyme","volume":"74","author":"Lu","year":"2007","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.1111\/j.1365-2672.2009.04291.x","article-title":"Production and synthetic dyes decolourization capacity of a recombinant laccase from Pichia pastoris","volume":"107","author":"Lu","year":"2009","journal-title":"J. Appl. Microbiol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1007\/s002530100687","article-title":"Biotechnological production of vanillin","volume":"56","author":"Priefert","year":"2001","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_65","unstructured":"Luque, R. (2011). Application of laccases in organic synthesis: A review. Green Chemistry, Nova Science Publishers, Inc."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1089\/cmb.2012.0021","article-title":"SPAdes: A new genome assembly algorithm and its applications to single-cell sequencing","volume":"19","author":"Bankevich","year":"2012","journal-title":"J. Comput. Biol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/S0304-4165(97)00117-7","article-title":"Electrochemical analysis of the interactions of laccase mediators with lignin model compounds","volume":"1379","author":"Bourbonnais","year":"1998","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/S0141-0229(97)00199-3","article-title":"Oxidation of polycyclic aromatic hydrocarbons (PAH) by laccase of Trametes versicolor","volume":"22","author":"Majcherczyk","year":"1998","journal-title":"Enzyme Microb. Technol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/17\/9593\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T06:56:18Z","timestamp":1760165778000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/17\/9593"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,9,4]]},"references-count":69,"journal-issue":{"issue":"17","published-online":{"date-parts":[[2021,9]]}},"alternative-id":["ijms22179593"],"URL":"https:\/\/doi.org\/10.3390\/ijms22179593","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,9,4]]}}}