{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,13]],"date-time":"2026-07-13T23:51:09Z","timestamp":1783986669627,"version":"3.55.0"},"reference-count":57,"publisher":"Springer Science and Business Media LLC","issue":"3","license":[{"start":{"date-parts":[[2022,1,27]],"date-time":"2022-01-27T00:00:00Z","timestamp":1643241600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2022,1,27]],"date-time":"2022-01-27T00:00:00Z","timestamp":1643241600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"crossref","award":["JP19K05560"],"award-info":[{"award-number":["JP19K05560"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100006134","name":"Foundation for Promotion of Material Science and Technology of Japan","doi-asserted-by":"publisher","award":["JPMJSP2106"],"award-info":[{"award-number":["JPMJSP2106"]}],"id":[{"id":"10.13039\/501100006134","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Biotechnol Lett"],"published-print":{"date-parts":[[2022,3]]},"DOI":"10.1007\/s10529-022-03224-3","type":"journal-article","created":{"date-parts":[[2022,1,26]],"date-time":"2022-01-26T22:02:42Z","timestamp":1643234562000},"page":"461-471","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Immobilization of Baeyer\u2013Villiger monooxygenase from acetone grown Fusarium sp."],"prefix":"10.1007","volume":"44","author":[{"given":"Michio","family":"Takagi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kotchakorn","family":"T.sriwong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ayaka","family":"Masuda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nozomi","family":"Kawaguchi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shusuke","family":"Fukui","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lan Huong","family":"Le Viet","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dai-ichiro","family":"Kato","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takashi","family":"Kitayama","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mikio","family":"Fujii","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Afifa Ayu","family":"Koesoema","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8934-8198","authenticated-orcid":false,"given":"Tomoko","family":"Matsuda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2022,1,27]]},"reference":[{"key":"3224_CR1","doi-asserted-by":"publisher","first-page":"402","DOI":"10.1016\/j.ijbiomac.2015.12.018","volume":"84","author":"C Altinkaynak","year":"2016","unstructured":"Altinkaynak C, Yilmaz I, Koksal Z et al (2016) Preparation of lactoperoxidase incorporated hybrid nanoflower and its excellent activity and stability. Int J Biol Macromol 84:402\u2013409. https:\/\/doi.org\/10.1016\/j.ijbiomac.2015.12.018","journal-title":"Int J Biol Macromol"},{"key":"3224_CR2","doi-asserted-by":"publisher","first-page":"108004","DOI":"10.1016\/j.bej.2021.108004","volume":"171","author":"KRA Are","year":"2021","unstructured":"Are KRA, Ohshima S, Koike Y et al (2021) Enzymatic direct carboxylation under supercritical CO2. Biochem Eng J 171:108004. https:\/\/doi.org\/10.1016\/j.bej.2021.108004","journal-title":"Biochem Eng J"},{"key":"3224_CR3","doi-asserted-by":"publisher","first-page":"110607","DOI":"10.1016\/j.mcat.2019.110607","volume":"479","author":"A Basso","year":"2019","unstructured":"Basso A, Serban S (2019) Industrial applications of immobilized enzymes\u2014A review. Mol Catal 479:110607. https:\/\/doi.org\/10.1016\/j.mcat.2019.110607","journal-title":"Mol Catal"},{"key":"3224_CR4","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2019.01453","author":"WG Birolli","year":"2019","unstructured":"Birolli WG, Lima RN, Porto ALM (2019) Applications of marine-derived microorganisms and their enzymes in biocatalysis and biotransformation, the underexplored potentials. Front Microbiol. https:\/\/doi.org\/10.3389\/fmicb.2019.01453","journal-title":"Front Microbiol"},{"key":"3224_CR5","doi-asserted-by":"publisher","unstructured":"Block H, Maertens B, Spriestersbach A et al (2009) Chapter 27 immobilized-metal affinity chromatography (IMAC). A review. Methods Enzymol 463:439\u2013473. https:\/\/doi.org\/10.1016\/S0076-6879(09)63027-5","DOI":"10.1016\/S0076-6879(09)63027-5"},{"key":"3224_CR6","doi-asserted-by":"publisher","first-page":"7453","DOI":"10.1021\/acs.joc.8b00468","volume":"83","author":"YK Bong","year":"2018","unstructured":"Bong YK, Song S, Nazor J et al (2018) Baeyer-Villiger monooxygenase-mediated synthesis of esomeprazole as an alternative for kagan sulfoxidation. J Org Chem 83:7453\u20137458. https:\/\/doi.org\/10.1021\/acs.joc.8b00468","journal-title":"J Org Chem"},{"key":"3224_CR7","doi-asserted-by":"publisher","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","volume":"254","author":"MM Bradford","year":"1976","unstructured":"Bradford MM (1976) A rapid and sensitive method for the quantitation microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 254:248\u2013254","journal-title":"Anal Biochem"},{"key":"3224_CR8","doi-asserted-by":"publisher","first-page":"11406","DOI":"10.1021\/acs.chemrev.7b00167","volume":"117","author":"KP Bryliakov","year":"2017","unstructured":"Bryliakov KP (2017) Catalytic asymmetric oxygenations with the environmentally benign oxidants H2O2 and O2. Chem Rev 117:11406\u201311459. https:\/\/doi.org\/10.1021\/acs.chemrev.7b00167","journal-title":"Chem Rev"},{"key":"3224_CR9","doi-asserted-by":"publisher","first-page":"9134","DOI":"10.1039\/c4cc02605e","volume":"50","author":"KE Cassimjee","year":"2014","unstructured":"Cassimjee KE, Kadow M, Wikmark Y et al (2014) A general protein purification and immobilization method on controlled porosity glass: biocatalytic applications. Chem Commun 50:9134\u20139137. https:\/\/doi.org\/10.1039\/c4cc02605e","journal-title":"Chem Commun"},{"key":"3224_CR10","doi-asserted-by":"publisher","first-page":"313","DOI":"10.1016\/S0165-022X(01)00206-8","volume":"49","author":"GS Chaga","year":"2001","unstructured":"Chaga GS (2001) Twenty-five years of immobilized metal ion affinity chromatography: past, present and future. J Biochem Biophys Methods 49:313\u2013334. https:\/\/doi.org\/10.1016\/S0165-022X(01)00206-8","journal-title":"J Biochem Biophys Methods"},{"key":"3224_CR11","doi-asserted-by":"publisher","first-page":"781","DOI":"10.1128\/jb.170.2.781-789.1988","volume":"170","author":"YC Chen","year":"1988","unstructured":"Chen YC, Peoples OP, Walsh CT (1988) Acinetobacter cyclohexanone monooxygenase: gene cloning and sequence determination. J Bacteriol 170:781\u2013789. https:\/\/doi.org\/10.1128\/jb.170.2.781-789.1988","journal-title":"J Bacteriol"},{"key":"3224_CR12","doi-asserted-by":"publisher","first-page":"134","DOI":"10.1016\/j.apcata.2018.12.036","volume":"572","author":"MAF Delgove","year":"2019","unstructured":"Delgove MAF, Valencia D, Sol\u00e9 J et al (2019) High performing immobilized Baeyer-Villiger monooxygenase and glucose dehydrogenase for the synthesis of \u03b5-caprolactone derivative. Appl Catal A Gen 572:134\u2013141. https:\/\/doi.org\/10.1016\/j.apcata.2018.12.036","journal-title":"Appl Catal A Gen"},{"key":"3224_CR13","doi-asserted-by":"publisher","first-page":"9238","DOI":"10.1002\/anie.201800343","volume":"57","author":"JJ Dong","year":"2018","unstructured":"Dong JJ, Fern\u00e1ndez-Fueyo E, Hollmann F et al (2018) Biocatalytic oxidation reactions: a chemist\u2019s perspective. Angew Chem Int Ed 57:9238\u20139261. https:\/\/doi.org\/10.1002\/anie.201800343","journal-title":"Angew Chem Int Ed"},{"key":"3224_CR14","doi-asserted-by":"publisher","first-page":"175","DOI":"10.1111\/j.1432-1033.1976.tb10220.x","volume":"63","author":"NA Donoghue","year":"1976","unstructured":"Donoghue NA, Norris DB, Trudgill PW (1976) The purification and properties of cyclohexanone oxygenase from nocardia globerula CL1 and acinetobacter NCIB 9871. Eur J Biochem 63:175\u2013192. https:\/\/doi.org\/10.1111\/j.1432-1033.1976.tb10220.x","journal-title":"Eur J Biochem"},{"key":"3224_CR15","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/s13568-018-0709-x","volume":"8","author":"OB Fordwour","year":"2018","unstructured":"Fordwour OB, Luka G, Hoorfar M, Wolthers KR (2018) Kinetic characterization of acetone monooxygenase from Gordonia sp. strain TY-5. AMB Express 8:1\u201313. https:\/\/doi.org\/10.1186\/s13568-018-0709-x","journal-title":"AMB Express"},{"key":"3224_CR16","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1016\/s0014-5793(02)02623-6","volume":"518","author":"MW Fraaije","year":"2002","unstructured":"Fraaije MW, Kamerbeek NM, van Berkel WJH, Janssen DB (2002) Identification of a Baeyer-Villiger monooxygenase sequence motif. FEBS Lett 518:43\u201347. https:\/\/doi.org\/10.1016\/s0014-5793(02)02623-6","journal-title":"FEBS Lett"},{"key":"3224_CR17","doi-asserted-by":"publisher","first-page":"22626","DOI":"10.1074\/jbc.M112.372177","volume":"287","author":"S Franceschini","year":"2012","unstructured":"Franceschini S, Van Beek HL, Pennetta A et al (2012) Exploring the structural basis of substrate preferences in Baeyer-Villiger monooxygenases: insight from steroid monooxygenase. J Biol Chem 287:22626\u201322634. https:\/\/doi.org\/10.1074\/jbc.M112.372177","journal-title":"J Biol Chem"},{"key":"3224_CR18","doi-asserted-by":"publisher","first-page":"1","DOI":"10.2147\/aabc.s8589","volume":"3","author":"S Franke","year":"2010","unstructured":"Franke S, Herfurth J, Hoffmann D (2010) Estimating affinities of calcium ions to proteins. Adv Appl Bioinform Chem 3:1\u20136. https:\/\/doi.org\/10.2147\/aabc.s8589","journal-title":"Adv Appl Bioinform Chem"},{"key":"3224_CR19","doi-asserted-by":"publisher","first-page":"11207","DOI":"10.1021\/acscatal.9b03396","volume":"9","author":"MJLJ F\u00fcrst","year":"2019","unstructured":"F\u00fcrst MJLJ, Gran-Scheuch A, Aalbers FS, Fraaije MW (2019) Baeyer-Villiger monooxygenases: tunable oxidative biocatalysts. ACS Catal 9:11207\u201311241. https:\/\/doi.org\/10.1021\/acscatal.9b03396","journal-title":"ACS Catal"},{"key":"3224_CR20","doi-asserted-by":"publisher","first-page":"627","DOI":"10.1021\/jacs.6b12246","volume":"139","author":"MJLJ F\u00fcrst","year":"2017","unstructured":"F\u00fcrst MJLJ, Savino S, Dudek HM et al (2017) Polycyclic ketone monooxygenase from the thermophilic fungus Thermothelomyces thermophila: a structurally distinct biocatalyst for bulky substrates. J Am Chem Soc 139:627\u2013630. https:\/\/doi.org\/10.1021\/jacs.6b12246","journal-title":"J Am Chem Soc"},{"key":"3224_CR21","doi-asserted-by":"publisher","first-page":"428","DOI":"10.1038\/nnano.2012.80","volume":"7","author":"J Ge","year":"2012","unstructured":"Ge J, Lei J, Zare RN (2012) Protein-inorganic hybrid nanoflowers. Nat Nanotechnol 7:428\u2013432. https:\/\/doi.org\/10.1038\/nnano.2012.80","journal-title":"Nat Nanotechnol"},{"key":"3224_CR22","doi-asserted-by":"publisher","first-page":"671","DOI":"10.1128\/JB.01578-06","volume":"189","author":"RP Hausinger","year":"2007","unstructured":"Hausinger RP (2007) New insights into acetone metabolism. J Bacteriol 189:671\u2013673. https:\/\/doi.org\/10.1128\/JB.01578-06","journal-title":"J Bacteriol"},{"key":"3224_CR23","doi-asserted-by":"publisher","first-page":"793","DOI":"10.1016\/j.rser.2018.04.103","volume":"91","author":"Y Hu","year":"2018","unstructured":"Hu Y, Dai L, Liu D et al (2018) Progress & prospect of metal-organic frameworks (MOFs) for enzyme immobilization (enzyme\/MOFs). Renew Sustain Energy Rev 91:793\u2013801. https:\/\/doi.org\/10.1016\/j.rser.2018.04.103","journal-title":"Renew Sustain Energy Rev"},{"key":"3224_CR24","doi-asserted-by":"publisher","first-page":"1655","DOI":"10.1007\/s10529-008-9729-y","volume":"30","author":"M Kawamoto","year":"2008","unstructured":"Kawamoto M, Utsukihara T, Abe C et al (2008) Biotransformation of (\u00b1)-2-methylcyclohexanone by fungi. Biotechnol Lett 30:1655\u20131660. https:\/\/doi.org\/10.1007\/s10529-008-9729-y","journal-title":"Biotechnol Lett"},{"key":"3224_CR25","first-page":"251","volume-title":"Organic reactions","author":"GR Know","year":"1993","unstructured":"Know GR (1993) The Baeyer-Villiger oxidation of ketones and aldehydes. In: Paquette LA (ed) Organic reactions. Wiley, New York, pp 251\u2013798"},{"key":"3224_CR26","doi-asserted-by":"publisher","first-page":"2897","DOI":"10.1007\/s00253-020-10440-2","volume":"104","author":"AA Koesoema","year":"2020","unstructured":"Koesoema AA, Standley DM, Senda T, Matsuda T (2020) Impact and relevance of alcohol dehydrogenase enantioselectivities on biotechnological applications. Appl Microbiol Biotechnol 104:2897\u20132909","journal-title":"Appl Microbiol Biotechnol"},{"key":"3224_CR27","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1021\/jo030253l","volume":"69","author":"BG Kyte","year":"2004","unstructured":"Kyte BG, Rouvi\u00e8re P, Cheng Q, Stewart JD (2004) Assessing the substrate selectivities and enantioselectivities of eight novel Baeyer-Villiger monooxygenases toward alkyl-substituted cyclohexanones. J Org Chem 69:12\u201317. https:\/\/doi.org\/10.1021\/jo030253l","journal-title":"J Org Chem"},{"key":"3224_CR28","doi-asserted-by":"publisher","first-page":"1620","DOI":"10.1016\/j.tetasy.2013.11.003","volume":"24","author":"F Leipold","year":"2013","unstructured":"Leipold F, Rudroff F, Mihovilovic MD, Bornscheuer UT (2013) The steroid monooxygenase from Rhodococcus rhodochrous; a versatile biocatalyst. Tetrahedron Asymmetry 24:1620\u20131624. https:\/\/doi.org\/10.1016\/j.tetasy.2013.11.003","journal-title":"Tetrahedron Asymmetry"},{"key":"3224_CR29","doi-asserted-by":"publisher","first-page":"705","DOI":"10.1007\/s00253-011-3670-z","volume":"94","author":"F Leipold","year":"2012","unstructured":"Leipold F, Wardenga R, Bornscheuer UT (2012) Cloning, expression and characterization of a eukaryotic cycloalkanone monooxygenase from Cylindrocarpon radicicola ATCC 11011. Appl Microbiol Biotechnol 94:705\u2013717. https:\/\/doi.org\/10.1007\/s00253-011-3670-z","journal-title":"Appl Microbiol Biotechnol"},{"key":"3224_CR30","doi-asserted-by":"publisher","first-page":"6236","DOI":"10.1039\/C3CS35511J","volume":"42","author":"A Liese","year":"2013","unstructured":"Liese A, Hilterhaus L (2013) Evaluation of immobilized enzymes for industrial applications. Chem Soc Rev 42:6236\u20136249. https:\/\/doi.org\/10.1039\/C3CS35511J","journal-title":"Chem Soc Rev"},{"key":"3224_CR31","doi-asserted-by":"publisher","first-page":"1015","DOI":"10.1002\/adsc.201901178","volume":"362","author":"C Liu","year":"2020","unstructured":"Liu C, Wen KG, Zeng XP, Peng YY (2020) Advances in chemocatalytic asymmetric Baeyer-Villiger oxidations. Adv Synth Catal 362:1015\u20131031. https:\/\/doi.org\/10.1002\/adsc.201901178","journal-title":"Adv Synth Catal"},{"key":"3224_CR32","doi-asserted-by":"publisher","first-page":"8753","DOI":"10.1039\/c5cc00318k","volume":"51","author":"F L\u00f3pez-Gallego","year":"2015","unstructured":"L\u00f3pez-Gallego F, Yate L (2015) Selective biomineralization of Co3(PO4)2-sponges triggered by His-tagged proteins: efficient heterogeneous biocatalysts for redox processes. Chem Commun 51:8753\u20138756. https:\/\/doi.org\/10.1039\/c5cc00318k","journal-title":"Chem Commun"},{"key":"3224_CR33","doi-asserted-by":"publisher","first-page":"1451","DOI":"10.1016\/j.enzmictec.2007.01.018","volume":"40","author":"C Mateo","year":"2007","unstructured":"Mateo C, Palomo JM, Fernandez-Lorente G et al (2007) Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzym Microb Technol 40:1451\u20131463. https:\/\/doi.org\/10.1016\/j.enzmictec.2007.01.018","journal-title":"Enzym Microb Technol"},{"key":"3224_CR34","volume-title":"Future directions in biocatalysis","year":"2017","unstructured":"Matsuda T (ed) (2017) Future directions in biocatalysis, 2nd edn. Elsevier, Amsterdam","edition":"2"},{"key":"3224_CR35","doi-asserted-by":"publisher","first-page":"205","DOI":"10.1080\/13102818.2015.1008192","volume":"29","author":"NR Mohamad","year":"2015","unstructured":"Mohamad NR, Marzuki NHC, Buang NA et al (2015) An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes. Biotechnol Biotechnol Equip 29:205\u2013220. https:\/\/doi.org\/10.1080\/13102818.2015.1008192","journal-title":"Biotechnol Biotechnol Equip"},{"key":"3224_CR36","doi-asserted-by":"publisher","first-page":"624","DOI":"10.1093\/oxfordjournals.jbchem.a022494","volume":"126","author":"S Morii","year":"1999","unstructured":"Morii S, Sawamoto S, Yamauchi Y et al (1999) Steroid monooxygenase of Rhodococcus rhodochrous: sequencing of the genomic DNA, and hyperexpression, purification, and characterization of the recombinant enzyme. J Biochem 126:624\u2013631. https:\/\/doi.org\/10.1093\/oxfordjournals.jbchem.a022494","journal-title":"J Biochem"},{"key":"3224_CR37","doi-asserted-by":"publisher","first-page":"119","DOI":"10.1016\/B978-0-444-63743-7.00006-8","volume-title":"Future directions in biocatalysis","author":"Q-T Nguyen","year":"2017","unstructured":"Nguyen Q-T, Mattevi A, Fraaije MW (2017) Chapter 6\u2014expanding the repertoire of flavoenzyme-based biocatalysis. In: Matsuda T (ed) Future directions in biocatalysis, 2nd edn. Elsevier, Amsterdam, pp 119\u2013133","edition":"2"},{"key":"3224_CR38","doi-asserted-by":"publisher","DOI":"10.1039\/B912850F","author":"S Omura","year":"2009","unstructured":"Omura S, Fukuyama T, Murakami Y et al (2009) Hydroruthenation triggered catalytic conversion of dialdehydes and keto aldehydes to lactones. Chem Commun. https:\/\/doi.org\/10.1039\/B912850F","journal-title":"Chem Commun"},{"key":"3224_CR39","doi-asserted-by":"publisher","first-page":"3615","DOI":"10.1016\/S0021-9258(18)99875-3","volume":"241","author":"MA Rahm","year":"1966","unstructured":"Rahm MA, Sih CJ (1966) Mechanisms of steroid oxidation by microorganisms. XI. Enzymatic cleavage of the pregnane side chain. J Biol Chem 241:3615\u20133623. https:\/\/doi.org\/10.1016\/S0021-9258(18)99875-3","journal-title":"J Biol Chem"},{"key":"3224_CR40","doi-asserted-by":"publisher","first-page":"156","DOI":"10.1016\/j.enzmictec.2009.04.008","volume":"45","author":"B Ratu","year":"2009","unstructured":"Ratu B, G\u0142adkowski W, Wawrze C (2009) New aspects of the application of fusarium strains to production of alkylsubstituted \u025b-lactones. Enzym Microb Technol 45:156\u2013163. https:\/\/doi.org\/10.1016\/j.enzmictec.2009.04.008","journal-title":"Enzym Microb Technol"},{"key":"3224_CR41","doi-asserted-by":"publisher","first-page":"1394","DOI":"10.1016\/j.biochi.2013.03.005","volume":"95","author":"J Rebehmed","year":"2013","unstructured":"Rebehmed J, Alphand V, de Berardinis V, de Brevern AG (2013) Evolution study of the Baeyer-Villiger monooxygenases enzyme family: functional importance of the highly conserved residues. Biochimie 95:1394\u20131402. https:\/\/doi.org\/10.1016\/j.biochi.2013.03.005","journal-title":"Biochimie"},{"key":"3224_CR42","doi-asserted-by":"publisher","first-page":"1393","DOI":"10.1007\/s10529-007-9401-y","volume":"29","author":"J Rehdorf","year":"2007","unstructured":"Rehdorf J, Kirschner A, Bornscheuer UT (2007) Cloning, expression and characterization of a Baeyer-Villiger monooxygenase from Pseudomonas putida KT2440. Biotechnol Lett 29:1393\u20131398. https:\/\/doi.org\/10.1007\/s10529-007-9401-y","journal-title":"Biotechnol Lett"},{"key":"3224_CR43","doi-asserted-by":"publisher","first-page":"1479","DOI":"10.1007\/s00253-011-3823-0","volume":"95","author":"A Riebel","year":"2012","unstructured":"Riebel A, Dudek HM, De Gonzalo G et al (2012) Expanding the set of rhodococcal Baeyer-Villiger monooxygenases by high-throughput cloning, expression and substrate screening. Appl Microbiol Biotechnol 95:1479\u20131489. https:\/\/doi.org\/10.1007\/s00253-011-3823-0","journal-title":"Appl Microbiol Biotechnol"},{"key":"3224_CR44","doi-asserted-by":"publisher","first-page":"801","DOI":"10.1021\/acs.chemrev.7b00203","volume":"118","author":"RA Sheldon","year":"2018","unstructured":"Sheldon RA, Woodley JM (2018) Role of biocatalysis in sustainable chemistry. Chem Rev 118:801\u2013838. https:\/\/doi.org\/10.1021\/acs.chemrev.7b00203","journal-title":"Chem Rev"},{"key":"3224_CR45","doi-asserted-by":"publisher","DOI":"10.1016\/j.bej.2021.108263","author":"K T.sriwong","year":"2021","unstructured":"T.sriwong K, Kamogawa R, Issasi CSC et al (2021) Geotrichum candidum acetophenone reductase immobilization on reduced graphene oxide: a promising biocatalyst for green asymmetric reduction of ketones. Biochem Eng J. https:\/\/doi.org\/10.1016\/j.bej.2021.108263","journal-title":"Biochem Eng J"},{"key":"3224_CR46","doi-asserted-by":"publisher","first-page":"30953","DOI":"10.1039\/d0ra03160g","volume":"10","author":"K T.sriwong","year":"2020","unstructured":"T.sriwong K, Koesoema AA, Matsuda T (2020) Organic-inorganic nanocrystal reductase to promote green asymmetric synthesis. RSC Adv 10:30953\u201330960. https:\/\/doi.org\/10.1039\/d0ra03160g","journal-title":"RSC Adv"},{"key":"3224_CR47","doi-asserted-by":"publisher","first-page":"109866","DOI":"10.1016\/j.enzmictec.2021.109866","volume":"150","author":"K T.sriwong","year":"2021","unstructured":"T.sriwong K, Ogura K, Hawari MA, Matsuda T (2021) Geotrichum candidum aldehyde dehydrogenase-inorganic nanocrystal with enhanced activity. Enzyme Microb Technol 150:109866. https:\/\/doi.org\/10.1016\/j.enzmictec.2021.109866","journal-title":"Enzyme Microb Technol"},{"key":"3224_CR48","doi-asserted-by":"publisher","first-page":"111784","DOI":"10.1016\/j.mcat.2021.111784","volume":"513","author":"S Wei","year":"2021","unstructured":"Wei S, Liu Y, Zhou J et al (2021) Two enantiocomplementary Baeyer-Villiger monooxygenases newly identified for asymmetric oxyfunctionalization of thioether. Mol Catal 513:111784. https:\/\/doi.org\/10.1016\/j.mcat.2021.111784","journal-title":"Mol Catal"},{"key":"3224_CR49","doi-asserted-by":"publisher","first-page":"325","DOI":"10.1099\/00221287-120-2-325","volume":"120","author":"WM Wiegant","year":"1980","unstructured":"Wiegant WM, De Bont JAM (1980) A new route for ethylene glycol metabolism in mycobacterium E44. J Gen Microbiol 120:325\u2013331. https:\/\/doi.org\/10.1099\/00221287-120-2-325","journal-title":"J Gen Microbiol"},{"key":"3224_CR50","doi-asserted-by":"publisher","first-page":"549","DOI":"10.1111\/j.1751-7915.2012.00337.x","volume":"5","author":"A Willetts","year":"2012","unstructured":"Willetts A, Joint I, Gilbert JA et al (2012) Isolation and initial characterization of a novel type of Baeyer-Villiger monooxygenase activity from a marine microorganism. Microb Biotechnol 5:549\u2013559. https:\/\/doi.org\/10.1111\/j.1751-7915.2012.00337.x","journal-title":"Microb Biotechnol"},{"key":"3224_CR51","doi-asserted-by":"publisher","first-page":"4","DOI":"10.1016\/1046-2023(92)90052-A","volume":"4","author":"JJ Winzerling","year":"1992","unstructured":"Winzerling JJ, Berna P, Porath J (1992) How to use immobilized affinity chromatography metal ion. METHODS A Companion Methods Enzymol 4:4\u201313. https:\/\/doi.org\/10.1016\/1046-2023(92)90052-A","journal-title":"METHODS A Companion Methods Enzymol"},{"key":"3224_CR52","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s41598-018-28575-8","volume":"8","author":"JM Woo","year":"2018","unstructured":"Woo JM, Jeon EY, Seo EJ et al (2018) Improving catalytic activity of the Baeyer-Villiger monooxygenase-based Escherichia coli biocatalysts for the overproduction of (Z)-11-(heptanoyloxy)undec-9-enoic acid from ricinoleic acid. Sci Rep 8:1\u201311. https:\/\/doi.org\/10.1038\/s41598-018-28575-8","journal-title":"Sci Rep"},{"key":"3224_CR53","doi-asserted-by":"publisher","DOI":"10.1002\/anie.202006648","author":"S Wu","year":"2020","unstructured":"Wu S, Snajdrova R, Moore JC et al (2020) Biocatalysis: enzymatic synthesis for industrial applications. Angew Chem Int Ed. https:\/\/doi.org\/10.1002\/anie.202006648","journal-title":"Angew Chem Int Ed"},{"key":"3224_CR54","doi-asserted-by":"publisher","first-page":"2295","DOI":"10.1039\/c4tb01697a","volume":"3","author":"Y Yin","year":"2015","unstructured":"Yin Y, Xiao Y, Lin G et al (2015) An enzyme-inorganic hybrid nanoflower based immobilized enzyme reactor with enhanced enzymatic activity. J Mater Chem B 3:2295\u20132300. https:\/\/doi.org\/10.1039\/c4tb01697a","journal-title":"J Mater Chem B"},{"key":"3224_CR55","doi-asserted-by":"publisher","first-page":"2357","DOI":"10.1039\/c7ra12940h","volume":"8","author":"J Yu","year":"2018","unstructured":"Yu J, Chen X, Jiang M et al (2018) Efficient promiscuous Knoevenagel condensation catalyzed by papain confined in Cu3(PO4)2 nanoflowers. RSC Adv 8:2357\u20132364. https:\/\/doi.org\/10.1039\/c7ra12940h","journal-title":"RSC Adv"},{"key":"3224_CR56","doi-asserted-by":"publisher","first-page":"299","DOI":"10.1016\/j.colsurfb.2015.04.033","volume":"130","author":"Y Yu","year":"2015","unstructured":"Yu Y, Fei X, Tian J et al (2015) Self-assembled enzyme\u2013inorganic hybrid nanoflowers and their application to enzyme purification. Colloids Surfaces B Biointerfaces 130:299\u2013304. https:\/\/doi.org\/10.1016\/j.colsurfb.2015.04.033","journal-title":"Colloids Surfaces B Biointerfaces"},{"key":"3224_CR57","doi-asserted-by":"publisher","first-page":"109408","DOI":"10.1016\/j.enzmictec.2019.109408","volume":"132","author":"Y Zhang","year":"2020","unstructured":"Zhang Y, Sun W, Elfeky NM et al (2020) Self-assembly of lipase hybrid nanoflowers with bifunctional Ca2+ for improved activity and stability. Enzyme Microb Technol 132:109408. https:\/\/doi.org\/10.1016\/j.enzmictec.2019.109408","journal-title":"Enzyme Microb Technol"}],"container-title":["Biotechnology Letters"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s10529-022-03224-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s10529-022-03224-3\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s10529-022-03224-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,9]],"date-time":"2022-04-09T11:09:47Z","timestamp":1649502587000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s10529-022-03224-3"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,1,27]]},"references-count":57,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2022,3]]}},"alternative-id":["3224"],"URL":"https:\/\/doi.org\/10.1007\/s10529-022-03224-3","relation":{"has-preprint":[{"id-type":"doi","id":"10.21203\/rs.3.rs-1062946\/v1","asserted-by":"object"}]},"ISSN":["0141-5492","1573-6776"],"issn-type":[{"value":"0141-5492","type":"print"},{"value":"1573-6776","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,1,27]]},"assertion":[{"value":"9 November 2021","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"11 January 2022","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"27 January 2022","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare that they have no conflict of interest.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}}]}}