{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,4]],"date-time":"2026-06-04T17:55:19Z","timestamp":1780595719374,"version":"3.54.1"},"reference-count":61,"publisher":"MDPI AG","issue":"13","license":[{"start":{"date-parts":[[2025,6,20]],"date-time":"2025-06-20T00:00:00Z","timestamp":1750377600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"the Centre for Biotechnology and Bioengineering (CeBiB)","award":["FB0001"],"award-info":[{"award-number":["FB0001"]}]},{"name":"the Centre for Biotechnology and Bioengineering (CeBiB)","award":["AFB240001"],"award-info":[{"award-number":["AFB240001"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The Atacama Desert is emerging as an unexpected source of microbial life and, thus, a source of bioactive compounds and novel enzymes. Baeyer\u2013Villiger monooxygenases (BVMOs), a subclass of flavin-dependent monooxygenases (FPMOs), have gained attention as promising biocatalysts for the biosynthesis of industrially relevant molecules for a wide range of applications, such as pharmaceuticals and polymers, among others. BVMOs catalyze the oxidation of ketones and cyclic ketones to esters and lactones, respectively, by using molecular oxygen and NAD(P)H. BVMOs may also catalyze heteroatoms oxidation including sulfoxidations and N-oxidations. This work aims to search for novel BVMOs in the genomes of new bacterial strains isolated from the Atacama Desert. Bioinformatic analysis led to the identification of 10 putative BVMOs, where the monooxygenase named MO-G35A was selected. Genome context showed, downstream of the MO-G35A, a gene encoding for an enzyme from the short-chain dehydrogenase\/reductase family, suggesting a closer redox loop between both enzymes. MO-G35A was successfully expressed in three Escherichia coli expression systems, where higher yields were achieved using the E. coli Shuffle T7 as host, suggesting that correct disulfide bond formation is necessary for correct folding. Enzyme characterization showed that it operates optimally at 35\u201338 \u00b0C, exhibiting a Km of 0.06 mM and a kcat of 0.15 s\u22121 for bicyclo [3.2.0] hept-2-en-6-one (BHC). Furthermore, the study revealed high stability in the presence of organic solvents, making it suitable for applications in various industrial processes, especially when the substrates have poor solubility in aqueous solutions. These results highlight the robustness and adaptability of enzymes in extreme environments, making them valuable candidates for biotechnological applications.<\/jats:p>","DOI":"10.3390\/ijms26135940","type":"journal-article","created":{"date-parts":[[2025,6,20]],"date-time":"2025-06-20T08:13:56Z","timestamp":1750407236000},"page":"5940","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Recombinant Expression and Characterization of a Novel Type I Baeyer\u2013Villiger Monooxygenase from a Streptomyces Strain Isolated from the Rhizosphere of the Atacama Desert Lupinus oreophilus"],"prefix":"10.3390","volume":"26","author":[{"given":"Carolina","family":"Gonz\u00e1lez","sequence":"first","affiliation":[{"name":"Centre for Biotechnology and Bioengineering (CeBiB), Department of Chemical Engineering, Biotechnology and Materials, University of Chile, Santiago 8370459, Chile"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0003-5789-8499","authenticated-orcid":false,"given":"Sebasti\u00e1n","family":"Rodr\u00edguez","sequence":"additional","affiliation":[{"name":"Centre for Biotechnology and Bioengineering (CeBiB), Department of Chemical Engineering, Biotechnology and Materials, University of Chile, Santiago 8370459, Chile"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jos\u00e9 Pablo","family":"Reyes-Godoy","sequence":"additional","affiliation":[{"name":"Centre for Biotechnology and Bioengineering (CeBiB), Department of Chemical Engineering, Biotechnology and Materials, University of Chile, Santiago 8370459, Chile"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2463-4820","authenticated-orcid":false,"given":"Valeria","family":"Razmilic","sequence":"additional","affiliation":[{"name":"Centre for Biotechnology and Bioengineering (CeBiB), Department of Chemical Engineering, Biotechnology and Materials, University of Chile, Santiago 8370459, Chile"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Irene","family":"Mart\u00ednez","sequence":"additional","affiliation":[{"name":"Centre for Biotechnology and Bioengineering (CeBiB), Department of Chemical Engineering, Biotechnology and Materials, University of Chile, Santiago 8370459, Chile"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,6,20]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1016\/j.abb.2013.12.005","article-title":"Flavin dependent monooxygenases","volume":"544","author":"Huijbers","year":"2014","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"37376","DOI":"10.1039\/C9RA07345K","article-title":"Genome-based analysis of the type II PKS biosynthesis pathway of xanthones in Streptomyces caelestis and their antifungal activity","volume":"9","author":"Liu","year":"2019","journal-title":"RSC Adv."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Deng, Y., Zhou, Q., Wu, Y., Chen, X., and Zhong, F. (2022). Properties and Mechanisms of Flavin-Dependent Monooxygenases and Their Applications in Natural Product Synthesis. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23052622"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1016\/j.jbiotec.2006.03.044","article-title":"Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts","volume":"124","author":"Kamerbeek","year":"2006","journal-title":"J. Biotechnol."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Paul, C.E., Eggerichs, D., Westphal, A.H., Tischler, D., and van Berkel, W.J.H. (2021). Flavoprotein monooxygenases: Versatile biocatalysts. Biotechnol. Adv., 51.","DOI":"10.1016\/j.biotechadv.2021.107712"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1039\/C8NP00054A","article-title":"Native roles of Baeyer\u2013Villiger monooxygenases in the microbial metabolism of natural compounds","volume":"36","author":"Tolmie","year":"2019","journal-title":"Nat. Prod. Rep."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1016\/j.bbrc.2019.03.114","article-title":"Structural basis for the selective addition of an oxygen atom to cyclic ketones by Baeyer-Villiger monooxygenase from Parvibaculum lavamentivorans","volume":"512","author":"Nguyen","year":"2019","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"2466","DOI":"10.1021\/cb400399b","article-title":"Molecular Insight into Substrate Recognition and Catalysis of Baeyer\u2013Villiger Monooxygenase MtmOIV, the Key Frame-Modifying Enzyme in the Biosynthesis of Anticancer Agent Mithramycin","volume":"8","author":"Bosserman","year":"2013","journal-title":"ACS Chem. Biol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1016\/j.cbpa.2009.11.017","article-title":"Baeyer\u2013Villiger monooxygenases: Recent advances and future challenges","volume":"14","author":"Dudek","year":"2010","journal-title":"Curr. Opin. Chem. Biol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.jbiotec.2010.01.021","article-title":"Monooxygenases as biocatalysts: Classification, mechanistic aspects and biotechnological applications","volume":"146","author":"Winkler","year":"2010","journal-title":"J. Biotechnol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"2049","DOI":"10.1002\/cbic.201800318","article-title":"Direct Access to Medium-Chain \u03b1,\u03c9-Dicarboxylic Acids by Using a Baeyer\u2013Villiger Monooxygenase of Abnormal Regioselectivity","volume":"19","author":"Yu","year":"2018","journal-title":"ChemBioChem"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1997","DOI":"10.1021\/acs.biochem.8b00169","article-title":"Biocatalytic Routes to Lactone Monomers for Polymer Production","volume":"57","author":"Messiha","year":"2018","journal-title":"Biochemistry"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"6135","DOI":"10.1016\/j.bmcl.2011.08.025","article-title":"Baeyer\u2013Villiger monooxygenases in aroma compound synthesis","volume":"21","author":"Fink","year":"2011","journal-title":"Bioorg Med. Chem. Lett."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/S0167-7799(03)00144-6","article-title":"Towards large-scale synthetic applications of Baeyer-Villiger monooxygenases","volume":"21","author":"Alphand","year":"2003","journal-title":"Trends Biotechnol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1124","DOI":"10.1021\/acs.oprd.0c00115","article-title":"Enzymatic Preparation of the Chiral (S)-Sulfoxide Drug Esomeprazole at Pilot-Scale Levels","volume":"24","author":"Xu","year":"2020","journal-title":"Org. Process Res. Dev."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"7699","DOI":"10.1007\/s00253-014-5932-z","article-title":"Biotechnological production of chiral organic sulfoxides: Current state and perspectives","volume":"98","author":"Matsui","year":"2014","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"3354","DOI":"10.1074\/jbc.M307770200","article-title":"The Prodrug Activator EtaA from Mycobacterium tuberculosis Is a Baeyer-Villiger Monooxygenase","volume":"279","author":"Fraaije","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"4165","DOI":"10.1021\/cr1003437","article-title":"Baeyer\u2212Villiger Monooxygenases: More Than Just Green Chemistry","volume":"111","author":"Leisch","year":"2011","journal-title":"Chem. Rev."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Willetts, A. (2023). Bicyclo[3.2.0]carbocyclic Molecules and Redox Biotransformations: The Evolution of Closed-Loop Artificial Linear Biocatalytic Cascades and Related Redox-Neutral Systems. Molecules, 28.","DOI":"10.3390\/molecules28217249"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"396","DOI":"10.12688\/f1000research.7432.1","article-title":"Extremophiles and biotechnology: Current uses and prospects","volume":"5","author":"Coker","year":"2016","journal-title":"F1000Research"},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Gran-Scheuch, A., Trajkovic, M., Parra, L., and Fraaije, M.W. (2018). Mining the Genome of Streptomyces leeuwenhoekii: Two New Type I Baeyer\u2013Villiger Monooxygenases From Atacama Desert. Front. Microbiol., 9.","DOI":"10.3389\/fmicb.2018.01609"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1007\/s00253-004-1749-5","article-title":"Discovery of a thermostable Baeyer\u2013Villiger monooxygenase by genome mining","volume":"66","author":"Fraaije","year":"2005","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"15852","DOI":"10.1002\/anie.201608951","article-title":"Characterization and Crystal Structure of a Robust Cyclohexanone Monooxygenase","volume":"55","author":"Romero","year":"2016","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Azua-Bustos, A., Gonz\u00e1lez-Silva, C., and Fair\u00e9n, A.G. (2022). The Atacama Desert in Northern Chile as an Analog Model of Mars. Front. Astron. Space Sci., 8.","DOI":"10.3389\/fspas.2021.810426"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1018","DOI":"10.1126\/science.1089143","article-title":"Mars-Like Soils in the Atacama Desert, Chile, and the Dry Limit of Microbial Life","volume":"302","author":"Rainey","year":"2003","journal-title":"Science"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1146\/annurev-micro-102215-095236","article-title":"The Atacama Desert: Technical Resources and the Growing Importance of Novel Microbial Diversity","volume":"70","author":"Bull","year":"2016","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Crits-Christoph, A., Robinson, C.K., Barnum, T., Fricke, W.F., Davila, A.F., Jedynak, B., McKay, C.P., and DiRuggiero, J. (2013). Colonization patterns of soil microbial communities in the Atacama Desert. Microbiome, 1.","DOI":"10.1186\/2049-2618-1-28"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1491","DOI":"10.1021\/np200320u","article-title":"Chaxamycins A\u2013D, Bioactive Ansamycins from a Hyper-arid Desert Streptomyces sp.","volume":"74","author":"Rateb","year":"2011","journal-title":"J. Nat. Prod."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1038\/s41429-017-0012-0","article-title":"Asenjonamides A\u2013C, antibacterial metabolites isolated from Streptomyces asenjonii strain KNN 42.f from an extreme-hyper arid Atacama Desert soil","volume":"71","author":"Abdelkader","year":"2018","journal-title":"J. Antibiot"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1467","DOI":"10.1007\/s10482-018-1030-z","article-title":"Natural product diversity of actinobacteria in the Atacama Desert","volume":"111","author":"Rateb","year":"2018","journal-title":"Antonie Van Leeuwenhoek"},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Amaresan, N., Kumar, K., Naik, J.H., Bapatla, K.G., and Mishra, R.K. (2018). Streptomyces in Plant Growth Promotion. New and Future Developments in Microbial Biotechnology and Bioengineering, Elsevier.","DOI":"10.1016\/B978-0-444-63994-3.00008-4"},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Guan, Y., and Chen, X. (2023). Recent Applications of Flavin-Dependent Monooxygenases in Biosynthesis, Pharmaceutical Development, and Environmental Science. Catalysts, 13.","DOI":"10.20944\/preprints202311.1600.v1"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.pep.2017.11.005","article-title":"Overcoming challenges for amplified expression of recombinant proteins using Escherichia coli","volume":"144","author":"Ahmad","year":"2018","journal-title":"Protein Expr. Purif."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Astakala, R.V., Preet, G., Milne, B.F., Tibyangye, J., Razmilic, V., Castro, J.F., Asenjo, J.A., Andrews, B., Ebel, R., and Jaspars, M. (2022). Mutactimycin AP, a New Mutactimycin Isolated from an Actinobacteria from the Atacama Desert. Molecules, 27.","DOI":"10.3390\/molecules27217185"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1675","DOI":"10.1093\/bbb\/zbab079","article-title":"Cloning, expression, and characterization of Baeyer\u2013Villiger monooxygenases from eukaryotic Exophiala jeanselmei strain KUFI-6N","volume":"85","author":"Yamamoto","year":"2021","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"ref_36","first-page":"1083","article-title":"The Analysis and Application of a Recombinant Monooxygenase Library as a Biocatalyst for the Baeyer-Villiger Reaction","volume":"17","author":"Park","year":"2007","journal-title":"J. Microbiol. Biotechnol."},{"key":"ref_37","first-page":"406","article-title":"The neighbor-joining method: A new method for reconstructing phylogenetic trees","volume":"4","author":"Saitou","year":"1987","journal-title":"Mol. Biol. Evol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"783","DOI":"10.2307\/2408678","article-title":"Confidence limits on phylogenies: An approach using the bootstrap","volume":"39","author":"Felsenstein","year":"1985","journal-title":"Evolution"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"2454","DOI":"10.1002\/pro.5560061119","article-title":"Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD\/NAD(P)H binding","volume":"6","author":"Eppink","year":"1997","journal-title":"Protein Sci."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/S0014-5793(02)02623-6","article-title":"Identification of a Baeyer\u2013Villiger monooxygenase sequence motif","volume":"518","author":"Fraaije","year":"2002","journal-title":"FEBS Lett."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1479","DOI":"10.1007\/s00253-011-3823-0","article-title":"Expanding the set of rhodococcal Baeyer\u2013Villiger monooxygenases by high-throughput cloning, expression and substrate screening","volume":"95","author":"Riebel","year":"2012","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.molcatb.2012.11.009","article-title":"Expanding the biocatalytic toolbox of flavoprotein monooxygenases from Rhodococcus jostii RHA1","volume":"88","author":"Riebel","year":"2013","journal-title":"J. Mol. Catal. B Enzym."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"7557","DOI":"10.1007\/s00253-017-8501-4","article-title":"Coupled reactions by coupled enzymes: Alcohol to lactone cascade with alcohol dehydrogenase\u2013cyclohexanone monooxygenase fusions","volume":"101","author":"Aalbers","year":"2017","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1653","DOI":"10.1002\/cbic.201800814","article-title":"Convergent Cascade Catalyzed by Monooxygenase\u2013Alcohol Dehydrogenase Fusion Applied in Organic Media","volume":"20","author":"Huang","year":"2019","journal-title":"ChemBioChem"},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Purwani, N.N., Martin, C., Savino, S., and Fraaije, M.W. (2021). Modular Assembly of Phosphite Dehydrogenase and Phenylacetone Monooxygenase for Tuning Cofactor Regeneration. Biomolecules, 11.","DOI":"10.3390\/biom11060905"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1016\/j.bbrc.2018.04.029","article-title":"SlyD-deficient Escherichia coli strains: A highway to contaminant-free protein extraction","volume":"499","author":"Mokhonov","year":"2018","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1186\/1475-2859-11-56","article-title":"SHuffle, a novel Escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasm","volume":"11","author":"Lobstein","year":"2012","journal-title":"Microb. Cell Fact."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"5.26.1","DOI":"10.1002\/cpps.11","article-title":"Use of the SHuffle Strains in Production of Proteins","volume":"85","author":"Ren","year":"2016","journal-title":"Curr. Protoc. Protein Sci."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Studier, F.W. (2018). T7 Expression Systems for Inducible Production of Proteins from Cloned Genes in E. coli. Curr. Protoc. Mol. Biol., 124.","DOI":"10.1002\/cpmb.63"},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Craig, D.B., and Dombkowski, A.A. (2013). Disulfide by Design 2.0: A web-based tool for disulfide engineering in proteins. BMC Bioinform., 14.","DOI":"10.1186\/1471-2105-14-346"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"19601","DOI":"10.1074\/jbc.274.28.19601","article-title":"Chaperone Activity of DsbC","volume":"274","author":"Chen","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1002\/cbic.201200006","article-title":"A Flavoprotein Monooxygenase that Catalyses a Baeyer\u2013Villiger Reaction and Thioether Oxidation Using NADH as the Nicotinamide Cofactor","volume":"13","author":"Jensen","year":"2012","journal-title":"ChemBioChem"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"110875","DOI":"10.1016\/j.mcat.2020.110875","article-title":"Genome mining reveals new bacterial type I Baeyer-Villiger monooxygenases with (bio)synthetic potential","volume":"486","author":"Ceccoli","year":"2020","journal-title":"Mol. Catal."},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"Niero, M., Righetto, I., Beneventi, E., de Laureto, P.P., Fraaije, M.W., Filippini, F., and Bergantino, E. (2020). Unique Features of a New Baeyer\u2013Villiger Monooxygenase from a Halophilic Archaeon. Catalysts, 10.","DOI":"10.3390\/catal10010128"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"2167","DOI":"10.1002\/bit.27022","article-title":"Stabilization of cyclohexanone monooxygenase by computational and experimental library design","volume":"116","author":"Boonstra","year":"2019","journal-title":"Biotechnol. Bioeng."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1186\/s13568-014-0023-1","article-title":"Cloning, expression and characterization of a versatile Baeyer-Villiger monooxygenase from Dietzia sp. D5","volume":"4","author":"Bisagni","year":"2014","journal-title":"AMB Express"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"3549","DOI":"10.1021\/acscatal.2c05160","article-title":"A Cold-Active Flavin-Dependent Monooxygenase from Janthinobacterium svalbardensis Unlocks Applications of Baeyer\u2013Villiger Monooxygenases at Low Temperature","volume":"13","author":"Polidori","year":"2023","journal-title":"ACS Catal."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1002\/bit.22963","article-title":"Effects of water miscible organic solvents on the activity and conformation of the baeyer\u2013villiger monooxygenases from Thermobifida fusca and Acinetobacter calcoaceticus: A comparative study","volume":"108","author":"Secundo","year":"2011","journal-title":"Biotechnol. Bioeng."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/j.bej.2009.09.009","article-title":"Organic solvent-tolerant enzymes","volume":"48","author":"Doukyu","year":"2010","journal-title":"Biochem. Eng. J."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"111784","DOI":"10.1016\/j.mcat.2021.111784","article-title":"Two enantiocomplementary Baeyer-Villiger monooxygenases newly identified for asymmetric oxyfunctionalization of thioether","volume":"513","author":"Wei","year":"2021","journal-title":"Mol. Catal."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"118531","DOI":"10.1016\/j.indcrop.2024.118531","article-title":"A sequential bioconversion-purification process to produce high purity xylo-oligosaccharides (XOS) from Nothophagus pumilio sawdust wastes","volume":"214","author":"Vera","year":"2024","journal-title":"Ind. Crops Prod."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/13\/5940\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T17:55:47Z","timestamp":1760032547000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/13\/5940"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,6,20]]},"references-count":61,"journal-issue":{"issue":"13","published-online":{"date-parts":[[2025,7]]}},"alternative-id":["ijms26135940"],"URL":"https:\/\/doi.org\/10.3390\/ijms26135940","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,6,20]]}}}