Partial purification and biochemical characterization of an alkaline esterase from Sorghum bicolor

Detalhes bibliográficos
Autor(a) principal: Gasparin, Fabiana Guillen Moreira
Data de Publicação: 2020
Outros Autores: Barros, Marcio de, Macedo, Gabriela Alves
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Acta Scientiarum Biological Sciences
Texto Completo: http://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSci/article/view/52115
Resumo: Esterases are enzymes that present good potential for industrial applications since they catalyze the formation or cleavage of ester bonds in water-soluble substrates, and sorghum seeds can represent an alternative source of this enzyme. The extraction of esterase from sorghum seeds is an economical alternative to obtain an enzyme of great interest. Esterases may improve the quality or accelerate the maturation of cheeses, cured bacon and fermented sausages and may also resolve racemic mixtures. Recently, seed esterases have been the focus of much attention as biocatalysts. In some cases, these enzymes present advantages over animal and microbial lipases due to some quite interesting features such as specificity and low cost, being a great alternative for their commercial exploitation as industrial enzymes The esterase studied here was extracted from sorghum seeds and some of its biochemical properties determined using synthetic substrates (p-nitrophenyl butyrate, caprylate, laurate and palmitate). The enzyme presented optimum activity at pH 8.0 and was stable in all the pH ranges studied. The optimum temperature for its activity was 40ºC but it showed low stability at this temperature (40% relative activity). The values derived for Km and Vmax were 0.67mM and 125 U.mg-1, respectively, obtained using p-nitrophenyl butyrate as the substrate. The enzyme showed an increase in activity when K2HPO4 was added to the reaction medium, but the ions Mn2+, CO+, Hg+ and Fe2+ strongly inhibited the enzyme activity. This enzyme showed a preference for the hydrolysis of short chain fatty acids. The characteristics of sorghum esterase are very similar to those of the microbial esterases used in detergent processing.
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spelling Partial purification and biochemical characterization of an alkaline esterase from Sorghum bicolorPartial purification and biochemical characterization of an alkaline esterase from Sorghum bicolorSorghum; esterase alkaline; biochemical characterization.Sorghum; esterase alkaline; biochemical characterization.Esterases are enzymes that present good potential for industrial applications since they catalyze the formation or cleavage of ester bonds in water-soluble substrates, and sorghum seeds can represent an alternative source of this enzyme. The extraction of esterase from sorghum seeds is an economical alternative to obtain an enzyme of great interest. Esterases may improve the quality or accelerate the maturation of cheeses, cured bacon and fermented sausages and may also resolve racemic mixtures. Recently, seed esterases have been the focus of much attention as biocatalysts. In some cases, these enzymes present advantages over animal and microbial lipases due to some quite interesting features such as specificity and low cost, being a great alternative for their commercial exploitation as industrial enzymes The esterase studied here was extracted from sorghum seeds and some of its biochemical properties determined using synthetic substrates (p-nitrophenyl butyrate, caprylate, laurate and palmitate). The enzyme presented optimum activity at pH 8.0 and was stable in all the pH ranges studied. The optimum temperature for its activity was 40ºC but it showed low stability at this temperature (40% relative activity). The values derived for Km and Vmax were 0.67mM and 125 U.mg-1, respectively, obtained using p-nitrophenyl butyrate as the substrate. The enzyme showed an increase in activity when K2HPO4 was added to the reaction medium, but the ions Mn2+, CO+, Hg+ and Fe2+ strongly inhibited the enzyme activity. This enzyme showed a preference for the hydrolysis of short chain fatty acids. The characteristics of sorghum esterase are very similar to those of the microbial esterases used in detergent processing.Esterases are enzymes that present good potential for industrial applications since they catalyze the formation or cleavage of ester bonds in water-soluble substrates, and sorghum seeds can represent an alternative source of this enzyme. The extraction of esterase from sorghum seeds is an economical alternative to obtain an enzyme of great interest. Esterases may improve the quality or accelerate the maturation of cheeses, cured bacon and fermented sausages and may also resolve racemic mixtures. Recently, seed esterases have been the focus of much attention as biocatalysts. In some cases, these enzymes present advantages over animal and microbial lipases due to some quite interesting features such as specificity and low cost, being a great alternative for their commercial exploitation as industrial enzymes The esterase studied here was extracted from sorghum seeds and some of its biochemical properties determined using synthetic substrates (p-nitrophenyl butyrate, caprylate, laurate and palmitate). The enzyme presented optimum activity at pH 8.0 and was stable in all the pH ranges studied. The optimum temperature for its activity was 40ºC but it showed low stability at this temperature (40% relative activity). The values derived for Km and Vmax were 0.67mM and 125 U.mg-1, respectively, obtained using p-nitrophenyl butyrate as the substrate. The enzyme showed an increase in activity when K2HPO4 was added to the reaction medium, but the ions Mn2+, CO+, Hg+ and Fe2+ strongly inhibited the enzyme activity. This enzyme showed a preference for the hydrolysis of short chain fatty acids. The characteristics of sorghum esterase are very similar to those of the microbial esterases used in detergent processing.Universidade Estadual De Maringá2020-08-27info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSci/article/view/5211510.4025/actascibiolsci.v42i1.52115Acta Scientiarum. Biological Sciences; Vol 42 (2020): Publicação contínua; e52115Acta Scientiarum. Biological Sciences; v. 42 (2020): Publicação contínua; e521151807-863X1679-9283reponame:Acta Scientiarum Biological Sciencesinstname:Universidade Estadual de Maringá (UEM)instacron:UEMenghttp://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSci/article/view/52115/751375150626Copyright (c) 2020 Acta Scientiarum. Biological Scienceshttp://creativecommons.org/licenses/by/4.0info:eu-repo/semantics/openAccess Gasparin, Fabiana Guillen Moreira Barros, Marcio deMacedo, Gabriela Alves2020-11-16T16:25:43Zoai:periodicos.uem.br/ojs:article/52115Revistahttp://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSciPUBhttp://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSci/oai||actabiol@uem.br1807-863X1679-9283opendoar:2020-11-16T16:25:43Acta Scientiarum Biological Sciences - Universidade Estadual de Maringá (UEM)false
dc.title.none.fl_str_mv Partial purification and biochemical characterization of an alkaline esterase from Sorghum bicolor
Partial purification and biochemical characterization of an alkaline esterase from Sorghum bicolor
title Partial purification and biochemical characterization of an alkaline esterase from Sorghum bicolor
spellingShingle Partial purification and biochemical characterization of an alkaline esterase from Sorghum bicolor
Gasparin, Fabiana Guillen Moreira
Sorghum; esterase alkaline; biochemical characterization.
Sorghum; esterase alkaline; biochemical characterization.
title_short Partial purification and biochemical characterization of an alkaline esterase from Sorghum bicolor
title_full Partial purification and biochemical characterization of an alkaline esterase from Sorghum bicolor
title_fullStr Partial purification and biochemical characterization of an alkaline esterase from Sorghum bicolor
title_full_unstemmed Partial purification and biochemical characterization of an alkaline esterase from Sorghum bicolor
title_sort Partial purification and biochemical characterization of an alkaline esterase from Sorghum bicolor
author Gasparin, Fabiana Guillen Moreira
author_facet Gasparin, Fabiana Guillen Moreira
Barros, Marcio de
Macedo, Gabriela Alves
author_role author
author2 Barros, Marcio de
Macedo, Gabriela Alves
author2_role author
author
dc.contributor.author.fl_str_mv Gasparin, Fabiana Guillen Moreira
Barros, Marcio de
Macedo, Gabriela Alves
dc.subject.por.fl_str_mv Sorghum; esterase alkaline; biochemical characterization.
Sorghum; esterase alkaline; biochemical characterization.
topic Sorghum; esterase alkaline; biochemical characterization.
Sorghum; esterase alkaline; biochemical characterization.
description Esterases are enzymes that present good potential for industrial applications since they catalyze the formation or cleavage of ester bonds in water-soluble substrates, and sorghum seeds can represent an alternative source of this enzyme. The extraction of esterase from sorghum seeds is an economical alternative to obtain an enzyme of great interest. Esterases may improve the quality or accelerate the maturation of cheeses, cured bacon and fermented sausages and may also resolve racemic mixtures. Recently, seed esterases have been the focus of much attention as biocatalysts. In some cases, these enzymes present advantages over animal and microbial lipases due to some quite interesting features such as specificity and low cost, being a great alternative for their commercial exploitation as industrial enzymes The esterase studied here was extracted from sorghum seeds and some of its biochemical properties determined using synthetic substrates (p-nitrophenyl butyrate, caprylate, laurate and palmitate). The enzyme presented optimum activity at pH 8.0 and was stable in all the pH ranges studied. The optimum temperature for its activity was 40ºC but it showed low stability at this temperature (40% relative activity). The values derived for Km and Vmax were 0.67mM and 125 U.mg-1, respectively, obtained using p-nitrophenyl butyrate as the substrate. The enzyme showed an increase in activity when K2HPO4 was added to the reaction medium, but the ions Mn2+, CO+, Hg+ and Fe2+ strongly inhibited the enzyme activity. This enzyme showed a preference for the hydrolysis of short chain fatty acids. The characteristics of sorghum esterase are very similar to those of the microbial esterases used in detergent processing.
publishDate 2020
dc.date.none.fl_str_mv 2020-08-27
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 http://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSci/article/view/52115
10.4025/actascibiolsci.v42i1.52115
url http://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSci/article/view/52115
identifier_str_mv 10.4025/actascibiolsci.v42i1.52115
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv http://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSci/article/view/52115/751375150626
dc.rights.driver.fl_str_mv Copyright (c) 2020 Acta Scientiarum. Biological Sciences
http://creativecommons.org/licenses/by/4.0
info:eu-repo/semantics/openAccess
rights_invalid_str_mv Copyright (c) 2020 Acta Scientiarum. Biological Sciences
http://creativecommons.org/licenses/by/4.0
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Universidade Estadual De Maringá
publisher.none.fl_str_mv Universidade Estadual De Maringá
dc.source.none.fl_str_mv Acta Scientiarum. Biological Sciences; Vol 42 (2020): Publicação contínua; e52115
Acta Scientiarum. Biological Sciences; v. 42 (2020): Publicação contínua; e52115
1807-863X
1679-9283
reponame:Acta Scientiarum Biological Sciences
instname:Universidade Estadual de Maringá (UEM)
instacron:UEM
instname_str Universidade Estadual de Maringá (UEM)
instacron_str UEM
institution UEM
reponame_str Acta Scientiarum Biological Sciences
collection Acta Scientiarum Biological Sciences
repository.name.fl_str_mv Acta Scientiarum Biological Sciences - Universidade Estadual de Maringá (UEM)
repository.mail.fl_str_mv ||actabiol@uem.br
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