Mono- and heterofunctionalized silica magnetic microparticles (SMMPs) as new carriers for immobilization of lipases

Detalhes bibliográficos
Autor(a) principal: de Lima, Lionete Nunes
Data de Publicação: 2016
Outros Autores: Vieira, Gustavo Nakamura Alves [UNESP], Kopp, Willian, Tardioli, Paulo Waldir, Giordano, Raquel L.C.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1016/j.molcatb.2017.04.002
http://hdl.handle.net/11449/174462
Resumo: In order to improve economic viability of an enzymatic process, the use of an operationally stable and low-cost biocatalyst is encouraged. Although the immobilization of lipases is widely reported, the search for new supports and immobilization protocols with better properties is still important. In this study, mono- and heterofunctionalized silica magnetic microparticles (SMMPs) were synthetized for immobilization of lipase B from Candida antarctica (CALB). The SMMPs were prepared in a micro-emulsion system containing sodium silicate and superparamagnetic iron oxide nanoparticles, followed by chemical modification with octyl groups and octyl plus aldehyde groups. These supports allowed the immobilization of CALB by hydrophobic adsorption or hydrophobic/covalent linkages, achieving immobilization yield of 88% and recovered activities of 128% and 59%, respectively. The performance of the magnetic biocatalysts was evaluated in the synthesis of xylose fatty acid esters (laurate or oleate) in tert-butyl alcohol medium, yielding around 60% conversion after 48 h under optimized conditions (xylose/fatty acid molar ratio of 1:0.2, 55 °C, and activity load of 37.5 U/g). The magnetic biocatalyst was used in 10 reaction cycles of 48 h at 46 °C maintaining high xylose conversions. Besides, the biocatalyst might be easily and quickly recovered from the reaction medium by an external magnetic field, an operational advantage in the case of viscous and complex media, e.g., medium containing insoluble sugars and molecular sieves.
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spelling Mono- and heterofunctionalized silica magnetic microparticles (SMMPs) as new carriers for immobilization of lipasesCandida antarctica lipase BHeterofunctionalizationSilica magnetic microparticlesXylose fatty acid esterIn order to improve economic viability of an enzymatic process, the use of an operationally stable and low-cost biocatalyst is encouraged. Although the immobilization of lipases is widely reported, the search for new supports and immobilization protocols with better properties is still important. In this study, mono- and heterofunctionalized silica magnetic microparticles (SMMPs) were synthetized for immobilization of lipase B from Candida antarctica (CALB). The SMMPs were prepared in a micro-emulsion system containing sodium silicate and superparamagnetic iron oxide nanoparticles, followed by chemical modification with octyl groups and octyl plus aldehyde groups. These supports allowed the immobilization of CALB by hydrophobic adsorption or hydrophobic/covalent linkages, achieving immobilization yield of 88% and recovered activities of 128% and 59%, respectively. The performance of the magnetic biocatalysts was evaluated in the synthesis of xylose fatty acid esters (laurate or oleate) in tert-butyl alcohol medium, yielding around 60% conversion after 48 h under optimized conditions (xylose/fatty acid molar ratio of 1:0.2, 55 °C, and activity load of 37.5 U/g). The magnetic biocatalyst was used in 10 reaction cycles of 48 h at 46 °C maintaining high xylose conversions. Besides, the biocatalyst might be easily and quickly recovered from the reaction medium by an external magnetic field, an operational advantage in the case of viscous and complex media, e.g., medium containing insoluble sugars and molecular sieves.Graduate Program in Chemical Engineering Department of Chemical Engineering Federal University of São Carlos, Rodovia Washington Luiz, km 235Department of Biochemistry and Chemical Technology Institute of Chemistry UNESP – São Paulo State UniversityKopp Technologies (KTech) Rua Alfredo Lopes, 1717, Jardim Macarengo, 13560-460Department of Biochemistry and Chemical Technology Institute of Chemistry UNESP – São Paulo State UniversityUniversidade Federal de São Carlos (UFSCar)Universidade Estadual Paulista (Unesp)Rua Alfredo Lopesde Lima, Lionete NunesVieira, Gustavo Nakamura Alves [UNESP]Kopp, WillianTardioli, Paulo WaldirGiordano, Raquel L.C.2018-12-11T17:11:14Z2018-12-11T17:11:14Z2016-10-29info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleS491-S499application/pdfhttp://dx.doi.org/10.1016/j.molcatb.2017.04.002Journal of Molecular Catalysis B: Enzymatic, v. 133, p. S491-S499.1873-31581381-1177http://hdl.handle.net/11449/17446210.1016/j.molcatb.2017.04.0022-s2.0-850174354862-s2.0-85017435486.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of Molecular Catalysis B: Enzymatic0,522info:eu-repo/semantics/openAccess2024-01-05T06:22:06Zoai:repositorio.unesp.br:11449/174462Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T22:09:32.423132Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Mono- and heterofunctionalized silica magnetic microparticles (SMMPs) as new carriers for immobilization of lipases
title Mono- and heterofunctionalized silica magnetic microparticles (SMMPs) as new carriers for immobilization of lipases
spellingShingle Mono- and heterofunctionalized silica magnetic microparticles (SMMPs) as new carriers for immobilization of lipases
de Lima, Lionete Nunes
Candida antarctica lipase B
Heterofunctionalization
Silica magnetic microparticles
Xylose fatty acid ester
title_short Mono- and heterofunctionalized silica magnetic microparticles (SMMPs) as new carriers for immobilization of lipases
title_full Mono- and heterofunctionalized silica magnetic microparticles (SMMPs) as new carriers for immobilization of lipases
title_fullStr Mono- and heterofunctionalized silica magnetic microparticles (SMMPs) as new carriers for immobilization of lipases
title_full_unstemmed Mono- and heterofunctionalized silica magnetic microparticles (SMMPs) as new carriers for immobilization of lipases
title_sort Mono- and heterofunctionalized silica magnetic microparticles (SMMPs) as new carriers for immobilization of lipases
author de Lima, Lionete Nunes
author_facet de Lima, Lionete Nunes
Vieira, Gustavo Nakamura Alves [UNESP]
Kopp, Willian
Tardioli, Paulo Waldir
Giordano, Raquel L.C.
author_role author
author2 Vieira, Gustavo Nakamura Alves [UNESP]
Kopp, Willian
Tardioli, Paulo Waldir
Giordano, Raquel L.C.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidade Federal de São Carlos (UFSCar)
Universidade Estadual Paulista (Unesp)
Rua Alfredo Lopes
dc.contributor.author.fl_str_mv de Lima, Lionete Nunes
Vieira, Gustavo Nakamura Alves [UNESP]
Kopp, Willian
Tardioli, Paulo Waldir
Giordano, Raquel L.C.
dc.subject.por.fl_str_mv Candida antarctica lipase B
Heterofunctionalization
Silica magnetic microparticles
Xylose fatty acid ester
topic Candida antarctica lipase B
Heterofunctionalization
Silica magnetic microparticles
Xylose fatty acid ester
description In order to improve economic viability of an enzymatic process, the use of an operationally stable and low-cost biocatalyst is encouraged. Although the immobilization of lipases is widely reported, the search for new supports and immobilization protocols with better properties is still important. In this study, mono- and heterofunctionalized silica magnetic microparticles (SMMPs) were synthetized for immobilization of lipase B from Candida antarctica (CALB). The SMMPs were prepared in a micro-emulsion system containing sodium silicate and superparamagnetic iron oxide nanoparticles, followed by chemical modification with octyl groups and octyl plus aldehyde groups. These supports allowed the immobilization of CALB by hydrophobic adsorption or hydrophobic/covalent linkages, achieving immobilization yield of 88% and recovered activities of 128% and 59%, respectively. The performance of the magnetic biocatalysts was evaluated in the synthesis of xylose fatty acid esters (laurate or oleate) in tert-butyl alcohol medium, yielding around 60% conversion after 48 h under optimized conditions (xylose/fatty acid molar ratio of 1:0.2, 55 °C, and activity load of 37.5 U/g). The magnetic biocatalyst was used in 10 reaction cycles of 48 h at 46 °C maintaining high xylose conversions. Besides, the biocatalyst might be easily and quickly recovered from the reaction medium by an external magnetic field, an operational advantage in the case of viscous and complex media, e.g., medium containing insoluble sugars and molecular sieves.
publishDate 2016
dc.date.none.fl_str_mv 2016-10-29
2018-12-11T17:11:14Z
2018-12-11T17:11:14Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1016/j.molcatb.2017.04.002
Journal of Molecular Catalysis B: Enzymatic, v. 133, p. S491-S499.
1873-3158
1381-1177
http://hdl.handle.net/11449/174462
10.1016/j.molcatb.2017.04.002
2-s2.0-85017435486
2-s2.0-85017435486.pdf
url http://dx.doi.org/10.1016/j.molcatb.2017.04.002
http://hdl.handle.net/11449/174462
identifier_str_mv Journal of Molecular Catalysis B: Enzymatic, v. 133, p. S491-S499.
1873-3158
1381-1177
10.1016/j.molcatb.2017.04.002
2-s2.0-85017435486
2-s2.0-85017435486.pdf
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Journal of Molecular Catalysis B: Enzymatic
0,522
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv S491-S499
application/pdf
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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