β-galactosidase Encapsulated in Carrageenan, Pectin and Carrageenan/Pectin: Comparative Study, Stability and Controlled Release

Detalhes bibliográficos
Autor(a) principal: SILVA,RENATA CRISTINA
Data de Publicação: 2020
Outros Autores: TREVISAN,MARCELLO G., GARCIA,JERUSA SIMONE
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Anais da Academia Brasileira de Ciências (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652020000100905
Resumo: Abstract The present study investigated the encapsulation of β-galactosidase in carrageenan, pectin and its hybrid hydrogels by using the ionotropic gelation method. The material obtained was characterized by Fourier transform infrared spectroscopy (FTIR), thermogravimetric analysis (TG/DTG) and scanning electron microscopy (SEM). The effects of pH, temperature and storage time were evaluated in terms of the catalytic activity of the free and encapsulated enzyme. Addition studies were conducted evaluating the performance of catalytic activity in vitro conditions. Carrageenan, pectin and hybrid hydrogels presented encapsulation efficiency of 58 ± 1%, 72 ± 1% and 77 ± 2%, respectively. The pectin hydrogel showed the higher β-galactosidase activity in pH and temperature tests. However, the carrageenan hydrogel exhibited best stability after been stored for three months. Carrageenan and pectin hydrogels were 2.0 and 2.4 times more efficiently than commercial tablet in the releasing β-galactosidase under in vitro conditions, respectively. The results suggest that pectin and carrageenan hydrogels may be useful for the development of new formulation of β-galactosidase.
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spelling β-galactosidase Encapsulated in Carrageenan, Pectin and Carrageenan/Pectin: Comparative Study, Stability and Controlled Releasebiopolymerencapsulationenzymatic activityionotropic gelationlactaseAbstract The present study investigated the encapsulation of β-galactosidase in carrageenan, pectin and its hybrid hydrogels by using the ionotropic gelation method. The material obtained was characterized by Fourier transform infrared spectroscopy (FTIR), thermogravimetric analysis (TG/DTG) and scanning electron microscopy (SEM). The effects of pH, temperature and storage time were evaluated in terms of the catalytic activity of the free and encapsulated enzyme. Addition studies were conducted evaluating the performance of catalytic activity in vitro conditions. Carrageenan, pectin and hybrid hydrogels presented encapsulation efficiency of 58 ± 1%, 72 ± 1% and 77 ± 2%, respectively. The pectin hydrogel showed the higher β-galactosidase activity in pH and temperature tests. However, the carrageenan hydrogel exhibited best stability after been stored for three months. Carrageenan and pectin hydrogels were 2.0 and 2.4 times more efficiently than commercial tablet in the releasing β-galactosidase under in vitro conditions, respectively. The results suggest that pectin and carrageenan hydrogels may be useful for the development of new formulation of β-galactosidase.Academia Brasileira de Ciências2020-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652020000100905Anais da Academia Brasileira de Ciências v.92 n.1 2020reponame:Anais da Academia Brasileira de Ciências (Online)instname:Academia Brasileira de Ciências (ABC)instacron:ABC10.1590/0001-3765202020180609info:eu-repo/semantics/openAccessSILVA,RENATA CRISTINATREVISAN,MARCELLO G.GARCIA,JERUSA SIMONEeng2020-03-31T00:00:00Zoai:scielo:S0001-37652020000100905Revistahttp://www.scielo.br/aabchttps://old.scielo.br/oai/scielo-oai.php||aabc@abc.org.br1678-26900001-3765opendoar:2020-03-31T00:00Anais da Academia Brasileira de Ciências (Online) - Academia Brasileira de Ciências (ABC)false
dc.title.none.fl_str_mv β-galactosidase Encapsulated in Carrageenan, Pectin and Carrageenan/Pectin: Comparative Study, Stability and Controlled Release
title β-galactosidase Encapsulated in Carrageenan, Pectin and Carrageenan/Pectin: Comparative Study, Stability and Controlled Release
spellingShingle β-galactosidase Encapsulated in Carrageenan, Pectin and Carrageenan/Pectin: Comparative Study, Stability and Controlled Release
SILVA,RENATA CRISTINA
biopolymer
encapsulation
enzymatic activity
ionotropic gelation
lactase
title_short β-galactosidase Encapsulated in Carrageenan, Pectin and Carrageenan/Pectin: Comparative Study, Stability and Controlled Release
title_full β-galactosidase Encapsulated in Carrageenan, Pectin and Carrageenan/Pectin: Comparative Study, Stability and Controlled Release
title_fullStr β-galactosidase Encapsulated in Carrageenan, Pectin and Carrageenan/Pectin: Comparative Study, Stability and Controlled Release
title_full_unstemmed β-galactosidase Encapsulated in Carrageenan, Pectin and Carrageenan/Pectin: Comparative Study, Stability and Controlled Release
title_sort β-galactosidase Encapsulated in Carrageenan, Pectin and Carrageenan/Pectin: Comparative Study, Stability and Controlled Release
author SILVA,RENATA CRISTINA
author_facet SILVA,RENATA CRISTINA
TREVISAN,MARCELLO G.
GARCIA,JERUSA SIMONE
author_role author
author2 TREVISAN,MARCELLO G.
GARCIA,JERUSA SIMONE
author2_role author
author
dc.contributor.author.fl_str_mv SILVA,RENATA CRISTINA
TREVISAN,MARCELLO G.
GARCIA,JERUSA SIMONE
dc.subject.por.fl_str_mv biopolymer
encapsulation
enzymatic activity
ionotropic gelation
lactase
topic biopolymer
encapsulation
enzymatic activity
ionotropic gelation
lactase
description Abstract The present study investigated the encapsulation of β-galactosidase in carrageenan, pectin and its hybrid hydrogels by using the ionotropic gelation method. The material obtained was characterized by Fourier transform infrared spectroscopy (FTIR), thermogravimetric analysis (TG/DTG) and scanning electron microscopy (SEM). The effects of pH, temperature and storage time were evaluated in terms of the catalytic activity of the free and encapsulated enzyme. Addition studies were conducted evaluating the performance of catalytic activity in vitro conditions. Carrageenan, pectin and hybrid hydrogels presented encapsulation efficiency of 58 ± 1%, 72 ± 1% and 77 ± 2%, respectively. The pectin hydrogel showed the higher β-galactosidase activity in pH and temperature tests. However, the carrageenan hydrogel exhibited best stability after been stored for three months. Carrageenan and pectin hydrogels were 2.0 and 2.4 times more efficiently than commercial tablet in the releasing β-galactosidase under in vitro conditions, respectively. The results suggest that pectin and carrageenan hydrogels may be useful for the development of new formulation of β-galactosidase.
publishDate 2020
dc.date.none.fl_str_mv 2020-01-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
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status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652020000100905
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652020000100905
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/0001-3765202020180609
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Academia Brasileira de Ciências
publisher.none.fl_str_mv Academia Brasileira de Ciências
dc.source.none.fl_str_mv Anais da Academia Brasileira de Ciências v.92 n.1 2020
reponame:Anais da Academia Brasileira de Ciências (Online)
instname:Academia Brasileira de Ciências (ABC)
instacron:ABC
instname_str Academia Brasileira de Ciências (ABC)
instacron_str ABC
institution ABC
reponame_str Anais da Academia Brasileira de Ciências (Online)
collection Anais da Academia Brasileira de Ciências (Online)
repository.name.fl_str_mv Anais da Academia Brasileira de Ciências (Online) - Academia Brasileira de Ciências (ABC)
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