Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350

Detalhes bibliográficos
Autor(a) principal: Pinheiro, Maísa Pessoa
Data de Publicação: 2017
Outros Autores: Cavalcante, Francisco Thálysson Tavares, Feitosa, Maria Rafaele Costa, Gonçalves, Luciana Rocha Barros, Santos, José Cleiton Sousa dos
Tipo de documento: Artigo de conferência
Idioma: por
Título da fonte: Repositório Institucional da Universidade Federal do Ceará (UFC)
Texto Completo: http://www.repositorio.ufc.br/handle/riufc/54437
Resumo: The strategy of enzyme immobilization is studied with the objective of producing more stable biocatalysts that can be used in reactions of high industrial interest. Lipase B from Candida antarctica (CALB) has been covalently immobilized on epoxy Immobead-350 (IB-350) and some properties have been compared to glyoxyl-agarose-CALB and Novozym 435. The thermal and solvent stability was higher than that of the glyoxyl-agarose-CALB, and the CALB-IB350 preparation was more stable at pH 5,0 and 70 °C (t1⁄2 = 68 min). The activity of the new preparation versus tributyrin and triacetin was about 4 and 17 fold higher than that of Novozym 435, respectively. Thus, the covalent attachment between enzyme and support produced a stable and active biocatalyst under different conditions and substrates.
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spelling Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350EnzimasLipaseLipase B Candida antarcticaThe strategy of enzyme immobilization is studied with the objective of producing more stable biocatalysts that can be used in reactions of high industrial interest. Lipase B from Candida antarctica (CALB) has been covalently immobilized on epoxy Immobead-350 (IB-350) and some properties have been compared to glyoxyl-agarose-CALB and Novozym 435. The thermal and solvent stability was higher than that of the glyoxyl-agarose-CALB, and the CALB-IB350 preparation was more stable at pH 5,0 and 70 °C (t1⁄2 = 68 min). The activity of the new preparation versus tributyrin and triacetin was about 4 and 17 fold higher than that of Novozym 435, respectively. Thus, the covalent attachment between enzyme and support produced a stable and active biocatalyst under different conditions and substrates.2020-10-02T18:29:16Z2020-10-02T18:29:16Z2017info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectapplication/pdfPINHEIRO, Maísa Pessoa; CAVALCANTE, Francisco Thálysson Tavares; FEITOSA, M. R. C.; GONÇALVES, Luciana Rocha Barros; SANTOS, José Cleiton Sousa dos. Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350. In: SIMPÓSIO NACIONAL DE BIOPROCESSOS, XXI; SIMPÓSIO DE HIDRÓLISE ENZIMÁTICA DE BIOMASSA, XII., 3 a 6 de set. 2017, Aracaju, Sergipe, Brasil. Anais [...] Aracaju, Sergipe, 2017.2447 2816http://www.repositorio.ufc.br/handle/riufc/54437Pinheiro, Maísa PessoaCavalcante, Francisco Thálysson TavaresFeitosa, Maria Rafaele CostaGonçalves, Luciana Rocha BarrosSantos, José Cleiton Sousa dosporreponame:Repositório Institucional da Universidade Federal do Ceará (UFC)instname:Universidade Federal do Ceará (UFC)instacron:UFCinfo:eu-repo/semantics/openAccess2023-07-04T19:02:43Zoai:repositorio.ufc.br:riufc/54437Repositório InstitucionalPUBhttp://www.repositorio.ufc.br/ri-oai/requestbu@ufc.br || repositorio@ufc.bropendoar:2024-09-11T18:58:42.391478Repositório Institucional da Universidade Federal do Ceará (UFC) - Universidade Federal do Ceará (UFC)false
dc.title.none.fl_str_mv Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350
Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350
title Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350
spellingShingle Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350
Pinheiro, Maísa Pessoa
Enzimas
Lipase
Lipase B Candida antarctica
title_short Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350
title_full Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350
title_fullStr Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350
title_full_unstemmed Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350
title_sort Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350
author Pinheiro, Maísa Pessoa
author_facet Pinheiro, Maísa Pessoa
Cavalcante, Francisco Thálysson Tavares
Feitosa, Maria Rafaele Costa
Gonçalves, Luciana Rocha Barros
Santos, José Cleiton Sousa dos
author_role author
author2 Cavalcante, Francisco Thálysson Tavares
Feitosa, Maria Rafaele Costa
Gonçalves, Luciana Rocha Barros
Santos, José Cleiton Sousa dos
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Pinheiro, Maísa Pessoa
Cavalcante, Francisco Thálysson Tavares
Feitosa, Maria Rafaele Costa
Gonçalves, Luciana Rocha Barros
Santos, José Cleiton Sousa dos
dc.subject.por.fl_str_mv Enzimas
Lipase
Lipase B Candida antarctica
topic Enzimas
Lipase
Lipase B Candida antarctica
description The strategy of enzyme immobilization is studied with the objective of producing more stable biocatalysts that can be used in reactions of high industrial interest. Lipase B from Candida antarctica (CALB) has been covalently immobilized on epoxy Immobead-350 (IB-350) and some properties have been compared to glyoxyl-agarose-CALB and Novozym 435. The thermal and solvent stability was higher than that of the glyoxyl-agarose-CALB, and the CALB-IB350 preparation was more stable at pH 5,0 and 70 °C (t1⁄2 = 68 min). The activity of the new preparation versus tributyrin and triacetin was about 4 and 17 fold higher than that of Novozym 435, respectively. Thus, the covalent attachment between enzyme and support produced a stable and active biocatalyst under different conditions and substrates.
publishDate 2017
dc.date.none.fl_str_mv 2017
2020-10-02T18:29:16Z
2020-10-02T18:29:16Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/conferenceObject
format conferenceObject
status_str publishedVersion
dc.identifier.uri.fl_str_mv PINHEIRO, Maísa Pessoa; CAVALCANTE, Francisco Thálysson Tavares; FEITOSA, M. R. C.; GONÇALVES, Luciana Rocha Barros; SANTOS, José Cleiton Sousa dos. Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350. In: SIMPÓSIO NACIONAL DE BIOPROCESSOS, XXI; SIMPÓSIO DE HIDRÓLISE ENZIMÁTICA DE BIOMASSA, XII., 3 a 6 de set. 2017, Aracaju, Sergipe, Brasil. Anais [...] Aracaju, Sergipe, 2017.
2447 2816
http://www.repositorio.ufc.br/handle/riufc/54437
identifier_str_mv PINHEIRO, Maísa Pessoa; CAVALCANTE, Francisco Thálysson Tavares; FEITOSA, M. R. C.; GONÇALVES, Luciana Rocha Barros; SANTOS, José Cleiton Sousa dos. Study of the stability and catalytic versatility of the lipase B from Candida antarctica immobilized on immobead-350. In: SIMPÓSIO NACIONAL DE BIOPROCESSOS, XXI; SIMPÓSIO DE HIDRÓLISE ENZIMÁTICA DE BIOMASSA, XII., 3 a 6 de set. 2017, Aracaju, Sergipe, Brasil. Anais [...] Aracaju, Sergipe, 2017.
2447 2816
url http://www.repositorio.ufc.br/handle/riufc/54437
dc.language.iso.fl_str_mv por
language por
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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