Imobilização da enzima ß-galactosidase em suporte de quitosana
Autor(a) principal: | |
---|---|
Data de Publicação: | 2022 |
Tipo de documento: | Dissertação |
Idioma: | por |
Título da fonte: | Biblioteca de teses e dissertações da Universidade de Passo Fundo (BDTD UPF) |
Texto Completo: | http://tede.upf.br:8080/jspui/handle/tede/2294 |
Resumo: | β-galactosidase enzyme has a great potential for application in the food industry due to its ability to carry out the hydrolysis of lactose, a disaccharide present in milk, whey, and dairy products. The enzyme can be used in the free form, in batch processes, or immobilized, allowing continuous operation and providing greater enzymatic stability. The choice of the method and the support for enzyme immobilization is fundamental since the performance of the biocatalyst is strongly influenced by the properties of the material used and by the mechanisms of interaction between support and enzyme. Physical adsorption is a simple and most commonly used immobilization method, and it can be reconciled with cross-linking. Allied to this, biopolymers are promising materials for enzymatic immobilization, mainly due to the non-toxicity and the availability of numerous reactive sites. Chitosan, due to its amine groups presents a strong interaction with the enzyme and can be used to form a composite with silica, to combine its properties and increase the stability of the immobilized enzyme. In this sense, this work aimed to evaluate the enzyme supports developed from chitosan for the immobilization of the β-galactosidase enzyme (Kluyveromyces lactis). For this, two approaches of the development of chitosan-based supports were evaluated. The first consists of a support developed by dropping chitosan solution into a coagulation solution containing 1 mol L-1 sodium hydroxide and 26% ethanol (v/v). The second is the synthesis of adsorbent composites based on chitosan and silica obtained by the sol-gel technique (xerogels). The xerogels were developed from different concentrations of glutaraldehyde to verify the influence of the crosslinking agent addition. Regarding the chitosan supports obtained by coagulation, the immobilization pH and the enzyme concentration were optimized for 6.0 and 5.0 mL L-1. Under these conditions, the immobilization efficiency and the degree of enzyme inactivation were 27% and 69%, respectively. After six cycles of reuse, the biocatalyst maintained 56% of immobilization efficiency. The support produced by the sol-gel technique (xerogel) showed immobilization efficiency between 15.83% and 17.38%. The crosslinking of chitosan with glutaraldehyde increased the degree of enzyme inactivation. However, crosslinking increased the immobilization efficiency up to a concentration of 2:1 (glutaraldehyde: chitosan monomer units, mol: mol). Therefore, the chitosan support obtained more promising results for the immobilization of the β-galactosidase than chitosan/silica xerogels. The results obtained attribute to the chitosan support developed an alternative to enable the use of the enzyme in the food industry. |
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Piccin, Jeferson SteffanelloCPF 00339280026http://lattes.cnpq.br/5392030005352784Fischer, JanaínaCPF 99822121091http://lattes.cnpq.br/7426402187639876CPF 03168746045http://lattes.cnpq.br/3080436833318536Damin, Brenda Isadora Soares2022-09-12T23:08:36Z2022-03-30DAMIN, Brenda Isadora Soares. Imobilização da enzima ß-galactosidase em suporte de quitosana. 2022. 60 f. Dissertação (Mestrado em Ciência e Tecnologia de Alimentos) - Universidade de Passo Fundo, Passo Fundo, RS, 2022.http://tede.upf.br:8080/jspui/handle/tede/2294β-galactosidase enzyme has a great potential for application in the food industry due to its ability to carry out the hydrolysis of lactose, a disaccharide present in milk, whey, and dairy products. The enzyme can be used in the free form, in batch processes, or immobilized, allowing continuous operation and providing greater enzymatic stability. The choice of the method and the support for enzyme immobilization is fundamental since the performance of the biocatalyst is strongly influenced by the properties of the material used and by the mechanisms of interaction between support and enzyme. Physical adsorption is a simple and most commonly used immobilization method, and it can be reconciled with cross-linking. Allied to this, biopolymers are promising materials for enzymatic immobilization, mainly due to the non-toxicity and the availability of numerous reactive sites. Chitosan, due to its amine groups presents a strong interaction with the enzyme and can be used to form a composite with silica, to combine its properties and increase the stability of the immobilized enzyme. In this sense, this work aimed to evaluate the enzyme supports developed from chitosan for the immobilization of the β-galactosidase enzyme (Kluyveromyces lactis). For this, two approaches of the development of chitosan-based supports were evaluated. The first consists of a support developed by dropping chitosan solution into a coagulation solution containing 1 mol L-1 sodium hydroxide and 26% ethanol (v/v). The second is the synthesis of adsorbent composites based on chitosan and silica obtained by the sol-gel technique (xerogels). The xerogels were developed from different concentrations of glutaraldehyde to verify the influence of the crosslinking agent addition. Regarding the chitosan supports obtained by coagulation, the immobilization pH and the enzyme concentration were optimized for 6.0 and 5.0 mL L-1. Under these conditions, the immobilization efficiency and the degree of enzyme inactivation were 27% and 69%, respectively. After six cycles of reuse, the biocatalyst maintained 56% of immobilization efficiency. The support produced by the sol-gel technique (xerogel) showed immobilization efficiency between 15.83% and 17.38%. The crosslinking of chitosan with glutaraldehyde increased the degree of enzyme inactivation. However, crosslinking increased the immobilization efficiency up to a concentration of 2:1 (glutaraldehyde: chitosan monomer units, mol: mol). Therefore, the chitosan support obtained more promising results for the immobilization of the β-galactosidase than chitosan/silica xerogels. The results obtained attribute to the chitosan support developed an alternative to enable the use of the enzyme in the food industry.A enzima β-galactosidase apresenta grande potencial de aplicação nas indústrias alimentícias, em decorrência de sua capacidade de realizar a hidrólise da lactose, dissacarídeo presente no leite, soro de leite e derivados lácteos. A enzima pode ser utilizada na forma livre, em processos em batelada, ou então na forma imobilizada, que permite operação contínua e proporciona maior estabilidade enzimática. A escolha do método e do suporte para imobilização da enzima é fundamental, pois o desempenho do biocatalisador é fortemente influenciado pelas propriedades do material empregado e pelos mecanismos de interação entre suporte e enzima. A adsorção física é um método de imobilização simples e mais comumente empregado, e pode ser conciliado com o cross-linking. Aliado a isso, os biopolímeros são materiais promissores para a imobilização enzimática, principalmente pela não toxicidade e disponibilidade de inúmeros locais reativos. A quitosana, pelos seus grupos aminas, apresenta forte interação com a enzima e pode ser proposta para formar compósito com sílica, afim de combinar suas propriedades e aumentar a estabilidade da enzima imobilizada. Nesse sentido, o objetivo do trabalho foi avaliar os suportes de enzimas desenvolvidos a partir de quitosana para a imobilização da enzima β-galactosidase (Kluyveromyces lactis). Para isso, duas abordagens de desenvolvimento de suportes a base de quitosana foram avaliadas. A primeira consiste em suporte desenvolvido por gotejamento de uma solução de quitosana em uma solução de coagulação contendo hidróxido de sódio 1 mol L-1 e etanol 26% (v/v). A segunda consiste na síntese de compósitos adsorventes a base de quitosana e sílica obtida pela técnica de sol-gel (xerogéis). Os xerogéis foram desenvolvidos a partir de diferentes concentrações de glutaraldeído para verificar a influência da adição do agente reticulante. Em relação aos suportes de quitosana obtidos por coagulação, o pH de imobilização e a concentração enzimática foram otimizados para 6,0 e 5,0 mL L-1. Nestas condições a eficiência de imobilização e o grau de inativação da enzima foram 27% e 69%, respectivamente. Após seis ciclos de reuso o biocatalisador manteve 56% de eficiência de imobilização. O suporte produzido pela técnica sol-gel (xerogel) apresentou eficiência de imobilização entre 15,83% e 17,38%. A reticulação da quitosana com glutaraldeído provocou aumentou o grau de inativação da enzima. Porém, até a concentração de 2:1 (glutaraldeído: unidades monoméricas de quitosana, mol: mol) a reticulação também aumentou a eficiência de imobilização. Diante disso, o suporte de quitosana obteve resultados mais promissores para imobilização da β-galactosidase em relação aos xerogéis de quitosana/sílica. Os resultados obtidos atribuem ao suporte de quitosana desenvolvido uma alternativa para viabilizar a utilização da enzima na indústria de alimentos.Submitted by Jucelei Domingues (jucelei@upf.br) on 2022-09-12T23:08:36Z No. of bitstreams: 1 2022BrendaIsadoraSoaresDamin.pdf: 1251353 bytes, checksum: 6bc2375dd00a8eb14b383a362989255d (MD5)Made available in DSpace on 2022-09-12T23:08:36Z (GMT). No. of bitstreams: 1 2022BrendaIsadoraSoaresDamin.pdf: 1251353 bytes, checksum: 6bc2375dd00a8eb14b383a362989255d (MD5) Previous issue date: 2022-03-30application/pdfporUniversidade de Passo FundoPrograma de Pós-Graduação em Ciência e Tecnologia de AlimentosUPFBrasilFaculdade de Agronomia e Medicina Veterinária – FAMVQuitosanaLactoseHidróliseCIENCIA E TECNOLOGIA DE ALIMENTOS::TECNOLOGIA DE ALIMENTOSImobilização da enzima ß-galactosidase em suporte de quitosanainfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesis-316835956343360854150050060053202200503672799-7636512811479495338info:eu-repo/semantics/openAccessreponame:Biblioteca de teses e dissertações da Universidade de Passo Fundo (BDTD UPF)instname:Universidade de Passo Fundo (UPF)instacron:UPFORIGINAL2022BrendaIsadoraSoaresDamin.pdf2022BrendaIsadoraSoaresDamin.pdfapplication/pdf1251353http://tede.upf.br:8080/jspui/bitstream/tede/2294/2/2022BrendaIsadoraSoaresDamin.pdf6bc2375dd00a8eb14b383a362989255dMD52LICENSElicense.txtlicense.txttext/plain; charset=utf-82053http://tede.upf.br:8080/jspui/bitstream/tede/2294/1/license.txt1ea0bfd7af108792edd8df732bb777fcMD51tede/22942022-09-12 20:08:36.921oai:tede.upf.br: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Biblioteca Digital de Teses e DissertaçõesPUBhttp://tede.upf.br/oai/requestbiblio@upf.br || bio@upf.br || cas@upf.br || car@upf.br || lve@upf.br || sar@upf.br || sol@upf.br || upfmundi@upf.br || jucelei@upf.bropendoar:2022-09-12T23:08:36Biblioteca de teses e dissertações da Universidade de Passo Fundo (BDTD UPF) - Universidade de Passo Fundo (UPF)false |
dc.title.por.fl_str_mv |
Imobilização da enzima ß-galactosidase em suporte de quitosana |
title |
Imobilização da enzima ß-galactosidase em suporte de quitosana |
spellingShingle |
Imobilização da enzima ß-galactosidase em suporte de quitosana Damin, Brenda Isadora Soares Quitosana Lactose Hidrólise CIENCIA E TECNOLOGIA DE ALIMENTOS::TECNOLOGIA DE ALIMENTOS |
title_short |
Imobilização da enzima ß-galactosidase em suporte de quitosana |
title_full |
Imobilização da enzima ß-galactosidase em suporte de quitosana |
title_fullStr |
Imobilização da enzima ß-galactosidase em suporte de quitosana |
title_full_unstemmed |
Imobilização da enzima ß-galactosidase em suporte de quitosana |
title_sort |
Imobilização da enzima ß-galactosidase em suporte de quitosana |
author |
Damin, Brenda Isadora Soares |
author_facet |
Damin, Brenda Isadora Soares |
author_role |
author |
dc.contributor.advisor1.fl_str_mv |
Piccin, Jeferson Steffanello |
dc.contributor.advisor1ID.fl_str_mv |
CPF 00339280026 |
dc.contributor.advisor1Lattes.fl_str_mv |
http://lattes.cnpq.br/5392030005352784 |
dc.contributor.advisor-co1.fl_str_mv |
Fischer, Janaína |
dc.contributor.advisor-co1ID.fl_str_mv |
CPF 99822121091 |
dc.contributor.advisor-co1Lattes.fl_str_mv |
http://lattes.cnpq.br/7426402187639876 |
dc.contributor.authorID.fl_str_mv |
CPF 03168746045 |
dc.contributor.authorLattes.fl_str_mv |
http://lattes.cnpq.br/3080436833318536 |
dc.contributor.author.fl_str_mv |
Damin, Brenda Isadora Soares |
contributor_str_mv |
Piccin, Jeferson Steffanello Fischer, Janaína |
dc.subject.por.fl_str_mv |
Quitosana Lactose Hidrólise |
topic |
Quitosana Lactose Hidrólise CIENCIA E TECNOLOGIA DE ALIMENTOS::TECNOLOGIA DE ALIMENTOS |
dc.subject.cnpq.fl_str_mv |
CIENCIA E TECNOLOGIA DE ALIMENTOS::TECNOLOGIA DE ALIMENTOS |
description |
β-galactosidase enzyme has a great potential for application in the food industry due to its ability to carry out the hydrolysis of lactose, a disaccharide present in milk, whey, and dairy products. The enzyme can be used in the free form, in batch processes, or immobilized, allowing continuous operation and providing greater enzymatic stability. The choice of the method and the support for enzyme immobilization is fundamental since the performance of the biocatalyst is strongly influenced by the properties of the material used and by the mechanisms of interaction between support and enzyme. Physical adsorption is a simple and most commonly used immobilization method, and it can be reconciled with cross-linking. Allied to this, biopolymers are promising materials for enzymatic immobilization, mainly due to the non-toxicity and the availability of numerous reactive sites. Chitosan, due to its amine groups presents a strong interaction with the enzyme and can be used to form a composite with silica, to combine its properties and increase the stability of the immobilized enzyme. In this sense, this work aimed to evaluate the enzyme supports developed from chitosan for the immobilization of the β-galactosidase enzyme (Kluyveromyces lactis). For this, two approaches of the development of chitosan-based supports were evaluated. The first consists of a support developed by dropping chitosan solution into a coagulation solution containing 1 mol L-1 sodium hydroxide and 26% ethanol (v/v). The second is the synthesis of adsorbent composites based on chitosan and silica obtained by the sol-gel technique (xerogels). The xerogels were developed from different concentrations of glutaraldehyde to verify the influence of the crosslinking agent addition. Regarding the chitosan supports obtained by coagulation, the immobilization pH and the enzyme concentration were optimized for 6.0 and 5.0 mL L-1. Under these conditions, the immobilization efficiency and the degree of enzyme inactivation were 27% and 69%, respectively. After six cycles of reuse, the biocatalyst maintained 56% of immobilization efficiency. The support produced by the sol-gel technique (xerogel) showed immobilization efficiency between 15.83% and 17.38%. The crosslinking of chitosan with glutaraldehyde increased the degree of enzyme inactivation. However, crosslinking increased the immobilization efficiency up to a concentration of 2:1 (glutaraldehyde: chitosan monomer units, mol: mol). Therefore, the chitosan support obtained more promising results for the immobilization of the β-galactosidase than chitosan/silica xerogels. The results obtained attribute to the chitosan support developed an alternative to enable the use of the enzyme in the food industry. |
publishDate |
2022 |
dc.date.accessioned.fl_str_mv |
2022-09-12T23:08:36Z |
dc.date.issued.fl_str_mv |
2022-03-30 |
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.citation.fl_str_mv |
DAMIN, Brenda Isadora Soares. Imobilização da enzima ß-galactosidase em suporte de quitosana. 2022. 60 f. Dissertação (Mestrado em Ciência e Tecnologia de Alimentos) - Universidade de Passo Fundo, Passo Fundo, RS, 2022. |
dc.identifier.uri.fl_str_mv |
http://tede.upf.br:8080/jspui/handle/tede/2294 |
identifier_str_mv |
DAMIN, Brenda Isadora Soares. Imobilização da enzima ß-galactosidase em suporte de quitosana. 2022. 60 f. Dissertação (Mestrado em Ciência e Tecnologia de Alimentos) - Universidade de Passo Fundo, Passo Fundo, RS, 2022. |
url |
http://tede.upf.br:8080/jspui/handle/tede/2294 |
dc.language.iso.fl_str_mv |
por |
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por |
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500 500 600 |
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53202200503672799 |
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dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
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openAccess |
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application/pdf |
dc.publisher.none.fl_str_mv |
Universidade de Passo Fundo |
dc.publisher.program.fl_str_mv |
Programa de Pós-Graduação em Ciência e Tecnologia de Alimentos |
dc.publisher.initials.fl_str_mv |
UPF |
dc.publisher.country.fl_str_mv |
Brasil |
dc.publisher.department.fl_str_mv |
Faculdade de Agronomia e Medicina Veterinária – FAMV |
publisher.none.fl_str_mv |
Universidade de Passo Fundo |
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Biblioteca de teses e dissertações da Universidade de Passo Fundo (BDTD UPF) |
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