Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves
Autor(a) principal: | |
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Data de Publicação: | 2022 |
Outros Autores: | , , , |
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=S0001-37652022000600501 |
Resumo: | Abstract Bromelia serra leaves collected from Corrientes, Argentina, were assessed to analyze and characterize the proteolytic system and to evaluate its potential use as an industrial catalyst. The specific activity of the enzymatic extract (EE), which was prepared using acetone as a precipitating agent of the crude extract (CE), increased 2-3 folds with different substrates (hemoglobin, azocasein and casein). The proteins present in the EE have isoelectric points between 4.55-8.15 and they were significant inhibited by pepstatin A (50%) and E-64 (15%). Proteolytic activity in EE presented high activity in acidic pH (2.7-4), and low activity in neutral alkaline pH (6-11.75). The EE optimum activity was reached at 60ºC, and referring to the thermal stability, it retained over 97% of the proteolytic activity after incubation at a temperature range of 37‒60 ºC for 60 min. The effect of reducing agents and ionic strength were also measured, and it showed that the EE had its maximum activity with 5mM of cysteine, and it was inactivated with 2.5 M of NaCl. The chromatography procedures presented two purified enzymes of 21 and 54 KDa with proteolytic activity. The characteristics of the EE suggest that it is a potential candidate as an industrial catalyst. |
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Proteolytic characterization of a novel enzymatic extract from Bromelia serra leavesAcidic proteaseBromelia serra leavesenzymatic extractsize-exclusion chromatographythermal stabilityAbstract Bromelia serra leaves collected from Corrientes, Argentina, were assessed to analyze and characterize the proteolytic system and to evaluate its potential use as an industrial catalyst. The specific activity of the enzymatic extract (EE), which was prepared using acetone as a precipitating agent of the crude extract (CE), increased 2-3 folds with different substrates (hemoglobin, azocasein and casein). The proteins present in the EE have isoelectric points between 4.55-8.15 and they were significant inhibited by pepstatin A (50%) and E-64 (15%). Proteolytic activity in EE presented high activity in acidic pH (2.7-4), and low activity in neutral alkaline pH (6-11.75). The EE optimum activity was reached at 60ºC, and referring to the thermal stability, it retained over 97% of the proteolytic activity after incubation at a temperature range of 37‒60 ºC for 60 min. The effect of reducing agents and ionic strength were also measured, and it showed that the EE had its maximum activity with 5mM of cysteine, and it was inactivated with 2.5 M of NaCl. The chromatography procedures presented two purified enzymes of 21 and 54 KDa with proteolytic activity. The characteristics of the EE suggest that it is a potential candidate as an industrial catalyst.Academia Brasileira de Ciências2022-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652022000600501Anais da Academia Brasileira de Ciências v.94 n.4 2022reponame:Anais da Academia Brasileira de Ciências (Online)instname:Academia Brasileira de Ciências (ABC)instacron:ABC10.1590/0001-3765202220201871info:eu-repo/semantics/openAccessHERRERA,MELANIE D. GÓMEZLUACES,PAULA ALAYÓNLIGGIERI,CONSTANZABRUNO,MARIELAAVANZA,MARÍA VICTORIAeng2022-08-02T00:00:00Zoai:scielo:S0001-37652022000600501Revistahttp://www.scielo.br/aabchttps://old.scielo.br/oai/scielo-oai.php||aabc@abc.org.br1678-26900001-3765opendoar:2022-08-02T00:00Anais da Academia Brasileira de Ciências (Online) - Academia Brasileira de Ciências (ABC)false |
dc.title.none.fl_str_mv |
Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves |
title |
Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves |
spellingShingle |
Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves HERRERA,MELANIE D. GÓMEZ Acidic protease Bromelia serra leaves enzymatic extract size-exclusion chromatography thermal stability |
title_short |
Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves |
title_full |
Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves |
title_fullStr |
Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves |
title_full_unstemmed |
Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves |
title_sort |
Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves |
author |
HERRERA,MELANIE D. GÓMEZ |
author_facet |
HERRERA,MELANIE D. GÓMEZ LUACES,PAULA ALAYÓN LIGGIERI,CONSTANZA BRUNO,MARIELA AVANZA,MARÍA VICTORIA |
author_role |
author |
author2 |
LUACES,PAULA ALAYÓN LIGGIERI,CONSTANZA BRUNO,MARIELA AVANZA,MARÍA VICTORIA |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
HERRERA,MELANIE D. GÓMEZ LUACES,PAULA ALAYÓN LIGGIERI,CONSTANZA BRUNO,MARIELA AVANZA,MARÍA VICTORIA |
dc.subject.por.fl_str_mv |
Acidic protease Bromelia serra leaves enzymatic extract size-exclusion chromatography thermal stability |
topic |
Acidic protease Bromelia serra leaves enzymatic extract size-exclusion chromatography thermal stability |
description |
Abstract Bromelia serra leaves collected from Corrientes, Argentina, were assessed to analyze and characterize the proteolytic system and to evaluate its potential use as an industrial catalyst. The specific activity of the enzymatic extract (EE), which was prepared using acetone as a precipitating agent of the crude extract (CE), increased 2-3 folds with different substrates (hemoglobin, azocasein and casein). The proteins present in the EE have isoelectric points between 4.55-8.15 and they were significant inhibited by pepstatin A (50%) and E-64 (15%). Proteolytic activity in EE presented high activity in acidic pH (2.7-4), and low activity in neutral alkaline pH (6-11.75). The EE optimum activity was reached at 60ºC, and referring to the thermal stability, it retained over 97% of the proteolytic activity after incubation at a temperature range of 37‒60 ºC for 60 min. The effect of reducing agents and ionic strength were also measured, and it showed that the EE had its maximum activity with 5mM of cysteine, and it was inactivated with 2.5 M of NaCl. The chromatography procedures presented two purified enzymes of 21 and 54 KDa with proteolytic activity. The characteristics of the EE suggest that it is a potential candidate as an industrial catalyst. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-01-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652022000600501 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652022000600501 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/0001-3765202220201871 |
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.94 n.4 2022 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) |
repository.mail.fl_str_mv |
||aabc@abc.org.br |
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1754302872466489344 |