Biocatalysts composed by lipase from thermomyces lanuginosus immobilized on superparamagnetic nanoparticles: design and application of lipase-nanoparticle biocatalysts in the synthesis of compounds used in different industrial fields

Detalhes bibliográficos
Autor(a) principal: Bezerra, Rayanne Mendes
Data de Publicação: 2018
Tipo de documento: Dissertação
Idioma: eng
Título da fonte: Repositório Institucional da Universidade Federal do Ceará (UFC)
Texto Completo: http://www.repositorio.ufc.br/handle/riufc/32256
Resumo: Lipase from Thermomyces lanuginosus (TLL) was immobilized on superparamagnetic iron oxide (Fe3O4) nanoparticles (SPMN) by different methods. Initially, the nanoparticles were prepared by the coprecipitation method. Then, the surface of magnetite was functionalized with polymers: 3-aminopropyltriethoxysilane (APTES) or branched polyethylenimine (PEI). Therefore, the enzyme immobilization was performed by two ways: by adsorption or by covalent attachment. In the adsorption way, the enzyme was immobilized by ionic affinity to the polymers attached to the SPMN surface. Previously the immobilization by covalent attachment, the support was activated with glutaraldehyde (GA) or divinylsulfone (DVS). Naturally, lipases catalyze the hydrolysis reactions. Thus, the developed biocatalysts were applied in some hydrolysis reactions of economic interest, for example, in the synthesis of a medicament precursor from the kinetic resolution of a racemate, obtaining the maximum conversion (50%) even after the second reaction cycle. However, lipases are able to catalyze esterification reactions in organic media; thus, the biocatalysts obtained after activation with DVS were applied in the esterification reaction of benzyl alcohol, obtaining up to 61% conversion after the seventh reaction cycle. Moreover, the preparations were characterized by different analysis: X-ray diffraction, vibrating sample magnetometry, infrared vibrational spectroscopy, zeta potential, among others. The SPMN presented superparamagnetic behavior even after the different enzymatic immobilization processes. The application conditions of the biocatalysts were also defined through studies of thermal, organic solvent, storage and operational stabilities. The DVS preparations had excellent operational stability, exhibiting more than 50% of the initial catalytic activity even after ten reaction cycles. On the other hand, the GA preparations presented greater thermal stability, reaching more than 7 hours of half-life at pH 7.0 at 70 °C. In general, these biocatalysts are thermostable, have high catalytic efficiency and good operational durability when applied under ideal reaction conditions. In addition, the economic interest reactions carried out in this work showed the potential applications of the developed biocatalysts in the pharmaceutical, cosmetic, biotechnology and fine chemical industries.
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spelling Biocatalysts composed by lipase from thermomyces lanuginosus immobilized on superparamagnetic nanoparticles: design and application of lipase-nanoparticle biocatalysts in the synthesis of compounds used in different industrial fieldsEngenharia químicaNanopartículasCatálise heterogêneaBiocatalisadoresEnzimas - SínteseSuperparamagnetic nanoparticlesThermomyces lanuginosus lipaseHeterogeneous catalysisEnzymatic synthesisLipase from Thermomyces lanuginosus (TLL) was immobilized on superparamagnetic iron oxide (Fe3O4) nanoparticles (SPMN) by different methods. Initially, the nanoparticles were prepared by the coprecipitation method. Then, the surface of magnetite was functionalized with polymers: 3-aminopropyltriethoxysilane (APTES) or branched polyethylenimine (PEI). Therefore, the enzyme immobilization was performed by two ways: by adsorption or by covalent attachment. In the adsorption way, the enzyme was immobilized by ionic affinity to the polymers attached to the SPMN surface. Previously the immobilization by covalent attachment, the support was activated with glutaraldehyde (GA) or divinylsulfone (DVS). Naturally, lipases catalyze the hydrolysis reactions. Thus, the developed biocatalysts were applied in some hydrolysis reactions of economic interest, for example, in the synthesis of a medicament precursor from the kinetic resolution of a racemate, obtaining the maximum conversion (50%) even after the second reaction cycle. However, lipases are able to catalyze esterification reactions in organic media; thus, the biocatalysts obtained after activation with DVS were applied in the esterification reaction of benzyl alcohol, obtaining up to 61% conversion after the seventh reaction cycle. Moreover, the preparations were characterized by different analysis: X-ray diffraction, vibrating sample magnetometry, infrared vibrational spectroscopy, zeta potential, among others. The SPMN presented superparamagnetic behavior even after the different enzymatic immobilization processes. The application conditions of the biocatalysts were also defined through studies of thermal, organic solvent, storage and operational stabilities. The DVS preparations had excellent operational stability, exhibiting more than 50% of the initial catalytic activity even after ten reaction cycles. On the other hand, the GA preparations presented greater thermal stability, reaching more than 7 hours of half-life at pH 7.0 at 70 °C. In general, these biocatalysts are thermostable, have high catalytic efficiency and good operational durability when applied under ideal reaction conditions. In addition, the economic interest reactions carried out in this work showed the potential applications of the developed biocatalysts in the pharmaceutical, cosmetic, biotechnology and fine chemical industries.Lipase de Thermomyces lanuginosus (TLL) foi imobilizada em nanopartículas superparamagnéticas (SPMN) de magnetita (Fe3O4) por diferentes métodos. Inicialmente, as nanopartículas foram sintetizadas pelo método de coprecipitação. Em seguida, a superfície dessas nanopartículas foi funcionalizada com polímeros: 3-aminopropiltrietoxisilano (APTES) ou polietilenoimina ramificada (PEI). Assim sendo, a imobilização da enzima ocorreu de duas formas: por adsorção ou por ligação covalente. Na adsorção, a enzima foi imobilizada por pseudo-afinidade aos polímeros ligados à superfície das SPMN. Antes da imobilização por ligação covalente, o suporte passou por uma etapa de ativação com glutaraldeído (GA) ou com divinilsulfona (DVS). Naturalmente, as lipases catalisam as reações de hidrólise. Logo, os biocatalisadores desenvolvidos foram aplicados em algumas reações de hidrólise de interesse econômico, como na síntese do intermediário de um fármaco a partir da resolução cinética de um racemato, obtendo a máxima conversão (50 %) mesmo após o segundo ciclo reacional. Entretanto, em meios orgânicos, as lipases são capazes de catalisar as reações de esterificação; assim sendo, os biocatalisadores obtidos após a ativação com DVS foram aplicados na reação de esterificação do álcool benzílico, obtendo até 61 % de conversão após o sétimo ciclo reacional. Além disso, os vários derivados foram caracterizados por diferentes análises: difração de raios X, magnetometria de amostra vibrante, espectroscopia vibracional no infravermelha, potencial zeta, entre outras. As SPMN apresentaram comportamento superparamagnético mesmo após os diferentes processos de imobilização enzimática. As condições de trabalho dos biocatalizadores também foram definidas através dos estudos de estabilidades térmica, em solvente orgânico, de estocagem e operacional. Os derivados ativados com DVS tiveram ótima estabilidade operacional, apresentando mais de 50% da atividade catalítica inicial mesmo após dez ciclos reacionais. Por outro lado, os derivados ativados com GA apresentaram maior estabilidade térmica, tendo alcançado mais de 7 horas de tempo de meia-vida em meio de pH 7.0 à 70 °C. De modo geral, esses biocatalisadores são termoestáveis, apresentam alta eficiência catalítica e boa durabilidade operacional quando aplicados dentro das condições ideais de reação. Ademais, as reações de interesse econômico realizadas neste trabalho mostraram o potencial de aplicação dos biocatalisadores desenvolvidos nas indústrias farmacêutica, cosmética, de biotecnologia e de química fina.Santos, José Cleiton Sousa dosGonçalves, Luciana Rocha BarrosBezerra, Rayanne Mendes2018-05-24T17:43:21Z2018-05-24T17:43:21Z2018info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisapplication/pdfBEZERRA, R. M. Biocatalysts composed by lipase from thermomyces lanuginosus immobilized on superparamagnetic nanoparticles: design and application of lipase-nanoparticle biocatalysts in the synthesis of compounds used in different industrial fields. 2018. 17 f. Dissertação (Mestrado em Engenharia Química) - Centro de Tecnologia, Universidade Federal do Ceará, Fortaleza, 2018.http://www.repositorio.ufc.br/handle/riufc/32256engreponame:Repositório Institucional da Universidade Federal do Ceará (UFC)instname:Universidade Federal do Ceará (UFC)instacron:UFCinfo:eu-repo/semantics/openAccess2020-10-02T17:19:01Zoai:repositorio.ufc.br:riufc/32256Repositório InstitucionalPUBhttp://www.repositorio.ufc.br/ri-oai/requestbu@ufc.br || repositorio@ufc.bropendoar:2020-10-02T17:19:01Repositório Institucional da Universidade Federal do Ceará (UFC) - Universidade Federal do Ceará (UFC)false
dc.title.none.fl_str_mv Biocatalysts composed by lipase from thermomyces lanuginosus immobilized on superparamagnetic nanoparticles: design and application of lipase-nanoparticle biocatalysts in the synthesis of compounds used in different industrial fields
title Biocatalysts composed by lipase from thermomyces lanuginosus immobilized on superparamagnetic nanoparticles: design and application of lipase-nanoparticle biocatalysts in the synthesis of compounds used in different industrial fields
spellingShingle Biocatalysts composed by lipase from thermomyces lanuginosus immobilized on superparamagnetic nanoparticles: design and application of lipase-nanoparticle biocatalysts in the synthesis of compounds used in different industrial fields
Bezerra, Rayanne Mendes
Engenharia química
Nanopartículas
Catálise heterogênea
Biocatalisadores
Enzimas - Síntese
Superparamagnetic nanoparticles
Thermomyces lanuginosus lipase
Heterogeneous catalysis
Enzymatic synthesis
title_short Biocatalysts composed by lipase from thermomyces lanuginosus immobilized on superparamagnetic nanoparticles: design and application of lipase-nanoparticle biocatalysts in the synthesis of compounds used in different industrial fields
title_full Biocatalysts composed by lipase from thermomyces lanuginosus immobilized on superparamagnetic nanoparticles: design and application of lipase-nanoparticle biocatalysts in the synthesis of compounds used in different industrial fields
title_fullStr Biocatalysts composed by lipase from thermomyces lanuginosus immobilized on superparamagnetic nanoparticles: design and application of lipase-nanoparticle biocatalysts in the synthesis of compounds used in different industrial fields
title_full_unstemmed Biocatalysts composed by lipase from thermomyces lanuginosus immobilized on superparamagnetic nanoparticles: design and application of lipase-nanoparticle biocatalysts in the synthesis of compounds used in different industrial fields
title_sort Biocatalysts composed by lipase from thermomyces lanuginosus immobilized on superparamagnetic nanoparticles: design and application of lipase-nanoparticle biocatalysts in the synthesis of compounds used in different industrial fields
author Bezerra, Rayanne Mendes
author_facet Bezerra, Rayanne Mendes
author_role author
dc.contributor.none.fl_str_mv Santos, José Cleiton Sousa dos
Gonçalves, Luciana Rocha Barros
dc.contributor.author.fl_str_mv Bezerra, Rayanne Mendes
dc.subject.por.fl_str_mv Engenharia química
Nanopartículas
Catálise heterogênea
Biocatalisadores
Enzimas - Síntese
Superparamagnetic nanoparticles
Thermomyces lanuginosus lipase
Heterogeneous catalysis
Enzymatic synthesis
topic Engenharia química
Nanopartículas
Catálise heterogênea
Biocatalisadores
Enzimas - Síntese
Superparamagnetic nanoparticles
Thermomyces lanuginosus lipase
Heterogeneous catalysis
Enzymatic synthesis
description Lipase from Thermomyces lanuginosus (TLL) was immobilized on superparamagnetic iron oxide (Fe3O4) nanoparticles (SPMN) by different methods. Initially, the nanoparticles were prepared by the coprecipitation method. Then, the surface of magnetite was functionalized with polymers: 3-aminopropyltriethoxysilane (APTES) or branched polyethylenimine (PEI). Therefore, the enzyme immobilization was performed by two ways: by adsorption or by covalent attachment. In the adsorption way, the enzyme was immobilized by ionic affinity to the polymers attached to the SPMN surface. Previously the immobilization by covalent attachment, the support was activated with glutaraldehyde (GA) or divinylsulfone (DVS). Naturally, lipases catalyze the hydrolysis reactions. Thus, the developed biocatalysts were applied in some hydrolysis reactions of economic interest, for example, in the synthesis of a medicament precursor from the kinetic resolution of a racemate, obtaining the maximum conversion (50%) even after the second reaction cycle. However, lipases are able to catalyze esterification reactions in organic media; thus, the biocatalysts obtained after activation with DVS were applied in the esterification reaction of benzyl alcohol, obtaining up to 61% conversion after the seventh reaction cycle. Moreover, the preparations were characterized by different analysis: X-ray diffraction, vibrating sample magnetometry, infrared vibrational spectroscopy, zeta potential, among others. The SPMN presented superparamagnetic behavior even after the different enzymatic immobilization processes. The application conditions of the biocatalysts were also defined through studies of thermal, organic solvent, storage and operational stabilities. The DVS preparations had excellent operational stability, exhibiting more than 50% of the initial catalytic activity even after ten reaction cycles. On the other hand, the GA preparations presented greater thermal stability, reaching more than 7 hours of half-life at pH 7.0 at 70 °C. In general, these biocatalysts are thermostable, have high catalytic efficiency and good operational durability when applied under ideal reaction conditions. In addition, the economic interest reactions carried out in this work showed the potential applications of the developed biocatalysts in the pharmaceutical, cosmetic, biotechnology and fine chemical industries.
publishDate 2018
dc.date.none.fl_str_mv 2018-05-24T17:43:21Z
2018-05-24T17:43:21Z
2018
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/masterThesis
format masterThesis
status_str publishedVersion
dc.identifier.uri.fl_str_mv BEZERRA, R. M. Biocatalysts composed by lipase from thermomyces lanuginosus immobilized on superparamagnetic nanoparticles: design and application of lipase-nanoparticle biocatalysts in the synthesis of compounds used in different industrial fields. 2018. 17 f. Dissertação (Mestrado em Engenharia Química) - Centro de Tecnologia, Universidade Federal do Ceará, Fortaleza, 2018.
http://www.repositorio.ufc.br/handle/riufc/32256
identifier_str_mv BEZERRA, R. M. Biocatalysts composed by lipase from thermomyces lanuginosus immobilized on superparamagnetic nanoparticles: design and application of lipase-nanoparticle biocatalysts in the synthesis of compounds used in different industrial fields. 2018. 17 f. Dissertação (Mestrado em Engenharia Química) - Centro de Tecnologia, Universidade Federal do Ceará, Fortaleza, 2018.
url http://www.repositorio.ufc.br/handle/riufc/32256
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Repositório Institucional da Universidade Federal do Ceará (UFC)
instname:Universidade Federal do Ceará (UFC)
instacron:UFC
instname_str Universidade Federal do Ceará (UFC)
instacron_str UFC
institution UFC
reponame_str Repositório Institucional da Universidade Federal do Ceará (UFC)
collection Repositório Institucional da Universidade Federal do Ceará (UFC)
repository.name.fl_str_mv Repositório Institucional da Universidade Federal do Ceará (UFC) - Universidade Federal do Ceará (UFC)
repository.mail.fl_str_mv bu@ufc.br || repositorio@ufc.br
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