Immobilization of protease extracted from Bacillus sp. P45 on different supports

Detalhes bibliográficos
Autor(a) principal: Reis, Daiane Felix
Data de Publicação: 2020
Outros Autores: Fadanni, Odivane, Brandelli, Adriano, Kalil, Susana Juliano
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Vetor (Online)
Texto Completo: https://periodicos.furg.br/vetor/article/view/7077
Resumo: Immobilization is a direct tool which not only improves the activity and stability of enzymes, but also enables their reuse. Therefore, selecting methods and supports to obtain biocatalysts with high selectivity and thermal stability is an important step. This study aimed at evaluating the immobilization of partially purified protease from Bacillus sp. P45, by different methods with the use of the following carriers: Amberlite IR® 120, montmorillonite clay, chitosan, glutaraldehyde-activated chitosan, Eupergit® C, DEAE-Cellulose® and QAE-Sephadex®. It also aimed at determining the operational stability of the derivative. The best results were obtained with the use of glutaraldehyde-activated chitosan, Amberlite IR® 120 and montmorillonite clay, with loading capacities of 25.4, 6.2 and 2.3 U/g support, respectively. Regarding the operational stability of the derivative glutaraldehyde-activated chitosan, the enzyme was found to keep 53.5% of its residual activity after being reused four times.
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spelling Immobilization of protease extracted from Bacillus sp. P45 on different supportsEnzimaImobilizaçãoAdsorçãoMatrizes.Immobilization is a direct tool which not only improves the activity and stability of enzymes, but also enables their reuse. Therefore, selecting methods and supports to obtain biocatalysts with high selectivity and thermal stability is an important step. This study aimed at evaluating the immobilization of partially purified protease from Bacillus sp. P45, by different methods with the use of the following carriers: Amberlite IR® 120, montmorillonite clay, chitosan, glutaraldehyde-activated chitosan, Eupergit® C, DEAE-Cellulose® and QAE-Sephadex®. It also aimed at determining the operational stability of the derivative. The best results were obtained with the use of glutaraldehyde-activated chitosan, Amberlite IR® 120 and montmorillonite clay, with loading capacities of 25.4, 6.2 and 2.3 U/g support, respectively. Regarding the operational stability of the derivative glutaraldehyde-activated chitosan, the enzyme was found to keep 53.5% of its residual activity after being reused four times.Universidade Federal do Rio Grande2020-06-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://periodicos.furg.br/vetor/article/view/7077VETOR - Journal of Exact Sciences and Engineering; Vol. 27 No. 2 (2017); 52-63VETOR - Revista de Ciências Exatas e Engenharias; v. 27 n. 2 (2017); 52-632358-34520102-7352reponame:Vetor (Online)instname:Universidade Federal do Rio Grande (FURG)instacron:FURGenghttps://periodicos.furg.br/vetor/article/view/7077/7424Copyright (c) 2020 VETOR - Revista de Ciências Exatas e Engenhariasinfo:eu-repo/semantics/openAccessReis, Daiane FelixFadanni, OdivaneBrandelli, AdrianoKalil, Susana Juliano2020-06-09T15:16:41Zoai:periodicos.furg.br:article/7077Revistahttps://periodicos.furg.br/vetorPUBhttps://periodicos.furg.br/vetor/oaigmplatt@furg.br2358-34520102-7352opendoar:2020-06-09T15:16:41Vetor (Online) - Universidade Federal do Rio Grande (FURG)false
dc.title.none.fl_str_mv Immobilization of protease extracted from Bacillus sp. P45 on different supports
title Immobilization of protease extracted from Bacillus sp. P45 on different supports
spellingShingle Immobilization of protease extracted from Bacillus sp. P45 on different supports
Reis, Daiane Felix
Enzima
Imobilização
Adsorção
Matrizes.
title_short Immobilization of protease extracted from Bacillus sp. P45 on different supports
title_full Immobilization of protease extracted from Bacillus sp. P45 on different supports
title_fullStr Immobilization of protease extracted from Bacillus sp. P45 on different supports
title_full_unstemmed Immobilization of protease extracted from Bacillus sp. P45 on different supports
title_sort Immobilization of protease extracted from Bacillus sp. P45 on different supports
author Reis, Daiane Felix
author_facet Reis, Daiane Felix
Fadanni, Odivane
Brandelli, Adriano
Kalil, Susana Juliano
author_role author
author2 Fadanni, Odivane
Brandelli, Adriano
Kalil, Susana Juliano
author2_role author
author
author
dc.contributor.author.fl_str_mv Reis, Daiane Felix
Fadanni, Odivane
Brandelli, Adriano
Kalil, Susana Juliano
dc.subject.por.fl_str_mv Enzima
Imobilização
Adsorção
Matrizes.
topic Enzima
Imobilização
Adsorção
Matrizes.
description Immobilization is a direct tool which not only improves the activity and stability of enzymes, but also enables their reuse. Therefore, selecting methods and supports to obtain biocatalysts with high selectivity and thermal stability is an important step. This study aimed at evaluating the immobilization of partially purified protease from Bacillus sp. P45, by different methods with the use of the following carriers: Amberlite IR® 120, montmorillonite clay, chitosan, glutaraldehyde-activated chitosan, Eupergit® C, DEAE-Cellulose® and QAE-Sephadex®. It also aimed at determining the operational stability of the derivative. The best results were obtained with the use of glutaraldehyde-activated chitosan, Amberlite IR® 120 and montmorillonite clay, with loading capacities of 25.4, 6.2 and 2.3 U/g support, respectively. Regarding the operational stability of the derivative glutaraldehyde-activated chitosan, the enzyme was found to keep 53.5% of its residual activity after being reused four times.
publishDate 2020
dc.date.none.fl_str_mv 2020-06-09
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://periodicos.furg.br/vetor/article/view/7077
url https://periodicos.furg.br/vetor/article/view/7077
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv https://periodicos.furg.br/vetor/article/view/7077/7424
dc.rights.driver.fl_str_mv Copyright (c) 2020 VETOR - Revista de Ciências Exatas e Engenharias
info:eu-repo/semantics/openAccess
rights_invalid_str_mv Copyright (c) 2020 VETOR - Revista de Ciências Exatas e Engenharias
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Universidade Federal do Rio Grande
publisher.none.fl_str_mv Universidade Federal do Rio Grande
dc.source.none.fl_str_mv VETOR - Journal of Exact Sciences and Engineering; Vol. 27 No. 2 (2017); 52-63
VETOR - Revista de Ciências Exatas e Engenharias; v. 27 n. 2 (2017); 52-63
2358-3452
0102-7352
reponame:Vetor (Online)
instname:Universidade Federal do Rio Grande (FURG)
instacron:FURG
instname_str Universidade Federal do Rio Grande (FURG)
instacron_str FURG
institution FURG
reponame_str Vetor (Online)
collection Vetor (Online)
repository.name.fl_str_mv Vetor (Online) - Universidade Federal do Rio Grande (FURG)
repository.mail.fl_str_mv gmplatt@furg.br
_version_ 1797041761757954048

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