Obtenção e performance de biocatalisadores: imobilização e efeito de aditivos químicos

Detalhes bibliográficos
Autor(a) principal: Torres, Juliana Arriel
Data de Publicação: 2017
Tipo de documento: Tese
Idioma: por
Título da fonte: Repositório Institucional da UFLA
Texto Completo: http://repositorio.ufla.br/jspui/handle/1/12932
Resumo: Peroxidases are enzymes with various applications, mainly in the degradation of organic compounds. Researches have been developed with these enzymes obtained from various vegetable sources, mainly agroindustrial waste. However, these biocatalysts are subject to inhibition, as for example by the final products of phenolic pollutants degradation. To overcome this limitation, chemical additives can be incorporated into the reaction medium, besides immobilizing these enzymes in different supports. In this work, were applied peroxidases obtained from turnip and soybeans, an agroindustrial residue, in the degradation of standard phenolic compounds in the presence of the additives polyethylene glycol (PEG) and triton X-100. It was evaluated also the degradation of total phenolic compounds from coffee processing wastewater (CPW) using soybean peroxidase (SP). In addition, another alternative was sought to improve the enzymatic stability, as well as to facilitate the removal of the biocatalyst and to enable the reuse of this, immobilizing this biocatalyst in activated carbon (AC), which was synthesized using the solid residue collected from the SP extraction. The immobilization of SP in AC (SP-AC) was evaluated at different time conditions, enzyme loading, pH and temperature. An activated carbon/magnetite composite was synthesized to facilitate the removal of the immobilized biocatalyst with the application of a magnetic field. Characterization techniques were performed in different materials. The turnip and soybean peroxidases were efficient in the degradation of the phenolic compounds, however, only for phenol and caffeic acid (pH 3.0), the protective effect of the additives was observed. PS presented 31.15% of CPW oxidation, however, in the presence of PEG and triton X-100 no influence on the oxidation of phenolic compounds was observed. The AC presented a high specific surface area of 1,603 m2 g-1, which makes it ideal for immobilization of enzymes, besides having been obtained with full use of biomass, with minimal waste generation. SP-AC immobilization reached 100% in the support:enzyme of 1.0:0.05 (m/m), pH 3.0, temperature 40 ° C for a period of 1 hour. SP-AC was reused for 10 cycles, presenting a decline in the first cycle and remaining constant until the last cycle. This drop may be associated with inhibition of the enzyme by the reaction products, once the enzyme has not been leached. Despite the advantage of using AC as a support for enzyme immobilization, its recovery from the reaction medium is a tedious process. To overcome this inconvenient a magnetic composite was synthesized. The immobilization of the magnetic SP-AC was 100% in the support:enzyme relationship of 1.0:0.05 (m/m), pH 3.0, temperature 50 ° C for a period of 7 hours. This magnetized immobilized biocatalyst was reused for 11 cycles, with a decrease of approximately 30% over the first cycle and remaining constant until the last. It is concluded that using additives in the oxidation of phenolic compounds of the CPW does not bring benefits, which represents a positive response from the economic point of view. The AC obtained represents a promising support for SP immobilization, with maximum biomass utilization, and the synthesized magnetic composite facilitates the recovery and reuse of the immobilized SP.
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spelling Obtenção e performance de biocatalisadores: imobilização e efeito de aditivos químicosObtaining and performance of biocatalysts: immobilization and the effect of chemical additivesEnzimas imobilizadasPeroxidaseCompostos fenólicosPolietilenoglicolCarvão ativadoMagnetitaResíduos agrícolasImmobilized enzymesPhenolic compoundsPolyethylene glycolActivated carbonMagnetiteAgricultural wastesTriton X-100Química OrgânicaPeroxidases are enzymes with various applications, mainly in the degradation of organic compounds. Researches have been developed with these enzymes obtained from various vegetable sources, mainly agroindustrial waste. However, these biocatalysts are subject to inhibition, as for example by the final products of phenolic pollutants degradation. To overcome this limitation, chemical additives can be incorporated into the reaction medium, besides immobilizing these enzymes in different supports. In this work, were applied peroxidases obtained from turnip and soybeans, an agroindustrial residue, in the degradation of standard phenolic compounds in the presence of the additives polyethylene glycol (PEG) and triton X-100. It was evaluated also the degradation of total phenolic compounds from coffee processing wastewater (CPW) using soybean peroxidase (SP). In addition, another alternative was sought to improve the enzymatic stability, as well as to facilitate the removal of the biocatalyst and to enable the reuse of this, immobilizing this biocatalyst in activated carbon (AC), which was synthesized using the solid residue collected from the SP extraction. The immobilization of SP in AC (SP-AC) was evaluated at different time conditions, enzyme loading, pH and temperature. An activated carbon/magnetite composite was synthesized to facilitate the removal of the immobilized biocatalyst with the application of a magnetic field. Characterization techniques were performed in different materials. The turnip and soybean peroxidases were efficient in the degradation of the phenolic compounds, however, only for phenol and caffeic acid (pH 3.0), the protective effect of the additives was observed. PS presented 31.15% of CPW oxidation, however, in the presence of PEG and triton X-100 no influence on the oxidation of phenolic compounds was observed. The AC presented a high specific surface area of 1,603 m2 g-1, which makes it ideal for immobilization of enzymes, besides having been obtained with full use of biomass, with minimal waste generation. SP-AC immobilization reached 100% in the support:enzyme of 1.0:0.05 (m/m), pH 3.0, temperature 40 ° C for a period of 1 hour. SP-AC was reused for 10 cycles, presenting a decline in the first cycle and remaining constant until the last cycle. This drop may be associated with inhibition of the enzyme by the reaction products, once the enzyme has not been leached. Despite the advantage of using AC as a support for enzyme immobilization, its recovery from the reaction medium is a tedious process. To overcome this inconvenient a magnetic composite was synthesized. The immobilization of the magnetic SP-AC was 100% in the support:enzyme relationship of 1.0:0.05 (m/m), pH 3.0, temperature 50 ° C for a period of 7 hours. This magnetized immobilized biocatalyst was reused for 11 cycles, with a decrease of approximately 30% over the first cycle and remaining constant until the last. It is concluded that using additives in the oxidation of phenolic compounds of the CPW does not bring benefits, which represents a positive response from the economic point of view. The AC obtained represents a promising support for SP immobilization, with maximum biomass utilization, and the synthesized magnetic composite facilitates the recovery and reuse of the immobilized SP.Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)As peroxidases são enzimas com várias aplicações, principalmente, na degradação de compostos orgânicos. Pesquisas têm sido desenvolvidas com estas enzimas obtidas de várias fontes vegetais, sobretudo de resíduos agroindustriais. Entretanto, estes biocatalisadores estão sujeitos à inibição, como por exemplo pelos produtos finais da degradação de poluentes fenólicos. Para contornar esta limitação se pode incorporar aditivos químicos no meio reacional, além de imobilizar estas enzimas em diferentes suportes. Neste trabalho, aplicou-se peroxidases obtidas do nabo e de cascas de soja, um resíduo agroindustrial, na degradação de compostos fenólicos padrões na presença dos aditivos polietilenoglicol (PEG) e triton X-100. Avaliou-se também a degradação de compostos fenólicos totais de águas residuárias do processamento do café (ARC) utilizando a peroxidase de soja (PS). Além disso, buscou-se outra alternativa para melhorar a estabilidade enzimática, bem como facilitar a remoção do biocatalisador e possibilitar a reutilização do mesmo, imobilizando este biocatalisador em carvão ativado (CA), que foi sintetizado empregando o resíduo sólido recolhido da extração da PS. A imobilização da PS em CA (PS-CA) foi avaliada em diferentes condições de tempo, carga de enzima, pH e temperatura. Sintetizou-se um compósito magnético carvão ativado/magnetita para facilitar a remoção do biocatalizador imobilizado, com a aplicação de um campo magnético. Técnicas de caracterização foram realizadas nos diferentes materiais. As peroxidases de nabo e soja foram eficientes na degradação dos compostos fenólicos, entretanto, apenas para o fenol e o ácido cafeico (pH 3,0), o efeito protetor dos aditivos foi observado. PS apresentou 31,15% de oxidação da ARC, entretanto, na presença de PEG e triton X-100 nenhuma influência na oxidação de compostos fenólicos foi observada. O CA apresentou elevada área superficial específica de 1.603 m2 g-1, que o torna ideal para imobilização de enzimas, além de ter sido obtido com aproveitamento total da biomassa, com geração mínima de resíduos. A imobilização PS-CA alcançou 100% na proporção suporte:enzima de 1,0:0,05 (m/m), pH 3,0, temperatura 40 °C por um período de 1 hora. PS-CA foi reutilizada durante 10 ciclos, apresentando um declínio no primeiro ciclo e mantendo-se constante até o último. Essa queda pode estar associada a inibição da enzima pelos produtos de reação, uma vez que a enzima não foi lixiviada. Apesar da vantagem de se utilizar o CA como suporte para imobilização de enzimas, sua recuperação do meio reacional é um processo tedioso. Para contornar este inconveniente sintetizou-se um compósito magnético. A imobilização da PS-CA magnético foi de 100% na proporção suporte:enzima de 1,0:0,05 (m/m), pH 3,0, temperatura 50 °C por um período de 7 horas. Esse biocatalisador imobilizado magnetizado foi reutilizado por 11 ciclos, com uma queda de aproximadamente 30% em relação ao primeiro ciclo e mantendo-se constante até o último. Conclui-se que utilizar aditivos na oxidação de compostos fenólicos da ARC não traz benefícios, o que representa uma resposta positiva do ponto de vista econômico. O CA obtido representa um suporte promissor para imobilização de PS, com aproveitamento máximo da biomassa, e o compósito magnético sintetizado facilita a recuperação e reutilização da PS imobilizada.Universidade Federal de LavrasPrograma de Pós-Graduação em AgroquímicaUFLAbrasilDepartamento de QuímicaCorrêa, Angelita DuarteSilva, Maria CristinaPereira, Chrystian AraújoLeal Neto, JonasBianchi, Maria LúciaSales, Priscila Ferreira deTorres, Juliana Arriel2017-05-10T14:29:20Z2017-05-10T14:29:20Z2017-05-102017-03-27info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/doctoralThesisapplication/pdfTORRES, J. A. Obtenção e performance de biocatalisadores: imobilização e efeito de aditivos químicos. 2017. 102 p. Tese (Doutorado em Agroquímica)-Universidade Federal de Lavras, Lavras, 2017.http://repositorio.ufla.br/jspui/handle/1/12932porinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UFLAinstname:Universidade Federal de Lavras (UFLA)instacron:UFLA2023-05-04T12:22:04Zoai:localhost:1/12932Repositório InstitucionalPUBhttp://repositorio.ufla.br/oai/requestnivaldo@ufla.br || repositorio.biblioteca@ufla.bropendoar:2023-05-04T12:22:04Repositório Institucional da UFLA - Universidade Federal de Lavras (UFLA)false
dc.title.none.fl_str_mv Obtenção e performance de biocatalisadores: imobilização e efeito de aditivos químicos
Obtaining and performance of biocatalysts: immobilization and the effect of chemical additives
title Obtenção e performance de biocatalisadores: imobilização e efeito de aditivos químicos
spellingShingle Obtenção e performance de biocatalisadores: imobilização e efeito de aditivos químicos
Torres, Juliana Arriel
Enzimas imobilizadas
Peroxidase
Compostos fenólicos
Polietilenoglicol
Carvão ativado
Magnetita
Resíduos agrícolas
Immobilized enzymes
Phenolic compounds
Polyethylene glycol
Activated carbon
Magnetite
Agricultural wastes
Triton X-100
Química Orgânica
title_short Obtenção e performance de biocatalisadores: imobilização e efeito de aditivos químicos
title_full Obtenção e performance de biocatalisadores: imobilização e efeito de aditivos químicos
title_fullStr Obtenção e performance de biocatalisadores: imobilização e efeito de aditivos químicos
title_full_unstemmed Obtenção e performance de biocatalisadores: imobilização e efeito de aditivos químicos
title_sort Obtenção e performance de biocatalisadores: imobilização e efeito de aditivos químicos
author Torres, Juliana Arriel
author_facet Torres, Juliana Arriel
author_role author
dc.contributor.none.fl_str_mv Corrêa, Angelita Duarte
Silva, Maria Cristina
Pereira, Chrystian Araújo
Leal Neto, Jonas
Bianchi, Maria Lúcia
Sales, Priscila Ferreira de
dc.contributor.author.fl_str_mv Torres, Juliana Arriel
dc.subject.por.fl_str_mv Enzimas imobilizadas
Peroxidase
Compostos fenólicos
Polietilenoglicol
Carvão ativado
Magnetita
Resíduos agrícolas
Immobilized enzymes
Phenolic compounds
Polyethylene glycol
Activated carbon
Magnetite
Agricultural wastes
Triton X-100
Química Orgânica
topic Enzimas imobilizadas
Peroxidase
Compostos fenólicos
Polietilenoglicol
Carvão ativado
Magnetita
Resíduos agrícolas
Immobilized enzymes
Phenolic compounds
Polyethylene glycol
Activated carbon
Magnetite
Agricultural wastes
Triton X-100
Química Orgânica
description Peroxidases are enzymes with various applications, mainly in the degradation of organic compounds. Researches have been developed with these enzymes obtained from various vegetable sources, mainly agroindustrial waste. However, these biocatalysts are subject to inhibition, as for example by the final products of phenolic pollutants degradation. To overcome this limitation, chemical additives can be incorporated into the reaction medium, besides immobilizing these enzymes in different supports. In this work, were applied peroxidases obtained from turnip and soybeans, an agroindustrial residue, in the degradation of standard phenolic compounds in the presence of the additives polyethylene glycol (PEG) and triton X-100. It was evaluated also the degradation of total phenolic compounds from coffee processing wastewater (CPW) using soybean peroxidase (SP). In addition, another alternative was sought to improve the enzymatic stability, as well as to facilitate the removal of the biocatalyst and to enable the reuse of this, immobilizing this biocatalyst in activated carbon (AC), which was synthesized using the solid residue collected from the SP extraction. The immobilization of SP in AC (SP-AC) was evaluated at different time conditions, enzyme loading, pH and temperature. An activated carbon/magnetite composite was synthesized to facilitate the removal of the immobilized biocatalyst with the application of a magnetic field. Characterization techniques were performed in different materials. The turnip and soybean peroxidases were efficient in the degradation of the phenolic compounds, however, only for phenol and caffeic acid (pH 3.0), the protective effect of the additives was observed. PS presented 31.15% of CPW oxidation, however, in the presence of PEG and triton X-100 no influence on the oxidation of phenolic compounds was observed. The AC presented a high specific surface area of 1,603 m2 g-1, which makes it ideal for immobilization of enzymes, besides having been obtained with full use of biomass, with minimal waste generation. SP-AC immobilization reached 100% in the support:enzyme of 1.0:0.05 (m/m), pH 3.0, temperature 40 ° C for a period of 1 hour. SP-AC was reused for 10 cycles, presenting a decline in the first cycle and remaining constant until the last cycle. This drop may be associated with inhibition of the enzyme by the reaction products, once the enzyme has not been leached. Despite the advantage of using AC as a support for enzyme immobilization, its recovery from the reaction medium is a tedious process. To overcome this inconvenient a magnetic composite was synthesized. The immobilization of the magnetic SP-AC was 100% in the support:enzyme relationship of 1.0:0.05 (m/m), pH 3.0, temperature 50 ° C for a period of 7 hours. This magnetized immobilized biocatalyst was reused for 11 cycles, with a decrease of approximately 30% over the first cycle and remaining constant until the last. It is concluded that using additives in the oxidation of phenolic compounds of the CPW does not bring benefits, which represents a positive response from the economic point of view. The AC obtained represents a promising support for SP immobilization, with maximum biomass utilization, and the synthesized magnetic composite facilitates the recovery and reuse of the immobilized SP.
publishDate 2017
dc.date.none.fl_str_mv 2017-05-10T14:29:20Z
2017-05-10T14:29:20Z
2017-05-10
2017-03-27
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/doctoralThesis
format doctoralThesis
status_str publishedVersion
dc.identifier.uri.fl_str_mv TORRES, J. A. Obtenção e performance de biocatalisadores: imobilização e efeito de aditivos químicos. 2017. 102 p. Tese (Doutorado em Agroquímica)-Universidade Federal de Lavras, Lavras, 2017.
http://repositorio.ufla.br/jspui/handle/1/12932
identifier_str_mv TORRES, J. A. Obtenção e performance de biocatalisadores: imobilização e efeito de aditivos químicos. 2017. 102 p. Tese (Doutorado em Agroquímica)-Universidade Federal de Lavras, Lavras, 2017.
url http://repositorio.ufla.br/jspui/handle/1/12932
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dc.publisher.none.fl_str_mv Universidade Federal de Lavras
Programa de Pós-Graduação em Agroquímica
UFLA
brasil
Departamento de Química
publisher.none.fl_str_mv Universidade Federal de Lavras
Programa de Pós-Graduação em Agroquímica
UFLA
brasil
Departamento de Química
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repository.name.fl_str_mv Repositório Institucional da UFLA - Universidade Federal de Lavras (UFLA)
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