Cell permeabilization of Kluyveromyces and Saccharomyces species to obtain potential biocatalysts for lactose hydrolysis
Autor(a) principal: | |
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Data de Publicação: | 2022 |
Outros Autores: | , , |
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/60336 |
Resumo: | Yeast’s beta-galactosidase is an intracellular enzyme, through which it is possible to determine in vivo its activity as a biocatalyst in the lactose hydrolysis. Permeabilization process was used for transforming the microorganisms cells into biocatalysts with an enhanced enzyme activity. The potential application of this enzyme technology in industrial process depends mainly on the enzyme activity. Beta-galactosidase enzyme that hydrolyzes lactose, for instance, is largely dependent on the reaction time and its stability under different physical conditions, such as pH, temperature and enzyme concentration. The objective of this study was to optimize the cellular permeabilization process of Kluyveromyces marxianus CCT 3172 and Saccharomyces fragilis CCT 7586 cultured in cheese whey for lactose hydrolysis. Box-Behnken design was carried out for cell permeabilization with three independent variables, ethanol concentration, permeabilization time and temperature. The best permeability conditions for K. marxianus CCT 3172 were 27% (v v-1) ethanol, 3 min at 20ºC, with specific enzymatic activity of 0.98 U mg-1. For S. fragilis CCT 7586, a specific enzymatic activity of 1.31 U mg-1 was achieved using 45% (v v-1) of ethanol, 17 min. of reaction under 17ºC. Thus, it was concluded that cellular permeabilization with ethanol is an efficient process to determine beta-galactosidase activity. |
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Cell permeabilization of Kluyveromyces and Saccharomyces species to obtain potential biocatalysts for lactose hydrolysisCell permeabilization of Kluyveromyces and Saccharomyces species to obtain potential biocatalysts for lactose hydrolysisbeta-galactosidase; cheese whey; lactose-hydrolysis; biocatalyst.beta-galactosidase; cheese whey; lactose-hydrolysis; biocatalyst.Yeast’s beta-galactosidase is an intracellular enzyme, through which it is possible to determine in vivo its activity as a biocatalyst in the lactose hydrolysis. Permeabilization process was used for transforming the microorganisms cells into biocatalysts with an enhanced enzyme activity. The potential application of this enzyme technology in industrial process depends mainly on the enzyme activity. Beta-galactosidase enzyme that hydrolyzes lactose, for instance, is largely dependent on the reaction time and its stability under different physical conditions, such as pH, temperature and enzyme concentration. The objective of this study was to optimize the cellular permeabilization process of Kluyveromyces marxianus CCT 3172 and Saccharomyces fragilis CCT 7586 cultured in cheese whey for lactose hydrolysis. Box-Behnken design was carried out for cell permeabilization with three independent variables, ethanol concentration, permeabilization time and temperature. The best permeability conditions for K. marxianus CCT 3172 were 27% (v v-1) ethanol, 3 min at 20ºC, with specific enzymatic activity of 0.98 U mg-1. For S. fragilis CCT 7586, a specific enzymatic activity of 1.31 U mg-1 was achieved using 45% (v v-1) of ethanol, 17 min. of reaction under 17ºC. Thus, it was concluded that cellular permeabilization with ethanol is an efficient process to determine beta-galactosidase activity.Yeast’s beta-galactosidase is an intracellular enzyme, through which it is possible to determine in vivo its activity as a biocatalyst in the lactose hydrolysis. Permeabilization process was used for transforming the microorganisms cells into biocatalysts with an enhanced enzyme activity. The potential application of this enzyme technology in industrial process depends mainly on the enzyme activity. Beta-galactosidase enzyme that hydrolyzes lactose, for instance, is largely dependent on the reaction time and its stability under different physical conditions, such as pH, temperature and enzyme concentration. The objective of this study was to optimize the cellular permeabilization process of Kluyveromyces marxianus CCT 3172 and Saccharomyces fragilis CCT 7586 cultured in cheese whey for lactose hydrolysis. Box-Behnken design was carried out for cell permeabilization with three independent variables, ethanol concentration, permeabilization time and temperature. The best permeability conditions for K. marxianus CCT 3172 were 27% (v v-1) ethanol, 3 min at 20ºC, with specific enzymatic activity of 0.98 U mg-1. For S. fragilis CCT 7586, a specific enzymatic activity of 1.31 U mg-1 was achieved using 45% (v v-1) of ethanol, 17 min. of reaction under 17ºC. Thus, it was concluded that cellular permeabilization with ethanol is an efficient process to determine beta-galactosidase activity.Universidade Estadual De Maringá2022-05-18info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSci/article/view/6033610.4025/actascibiolsci.v44i1.60336Acta Scientiarum. Biological Sciences; Vol 44 (2022): Publicação contínua; e60336Acta Scientiarum. Biological Sciences; v. 44 (2022): Publicação contínua; e603361807-863X1679-9283reponame:Acta Scientiarum Biological Sciencesinstname:Universidade Estadual de Maringá (UEM)instacron:UEMenghttp://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSci/article/view/60336/751375154205Copyright (c) 2022 Acta Scientiarum. Biological Scienceshttp://creativecommons.org/licenses/by/4.0info:eu-repo/semantics/openAccess Alves, Érika de PáduaBosso, Alessandra Morioka, Luiz Rodrigo ItoSuguimoto, Hélio Hiroshi 2022-06-22T14:07:51Zoai:periodicos.uem.br/ojs:article/60336Revistahttp://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSciPUBhttp://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSci/oai||actabiol@uem.br1807-863X1679-9283opendoar:2022-06-22T14:07:51Acta Scientiarum Biological Sciences - Universidade Estadual de Maringá (UEM)false |
dc.title.none.fl_str_mv |
Cell permeabilization of Kluyveromyces and Saccharomyces species to obtain potential biocatalysts for lactose hydrolysis Cell permeabilization of Kluyveromyces and Saccharomyces species to obtain potential biocatalysts for lactose hydrolysis |
title |
Cell permeabilization of Kluyveromyces and Saccharomyces species to obtain potential biocatalysts for lactose hydrolysis |
spellingShingle |
Cell permeabilization of Kluyveromyces and Saccharomyces species to obtain potential biocatalysts for lactose hydrolysis Alves, Érika de Pádua beta-galactosidase; cheese whey; lactose-hydrolysis; biocatalyst. beta-galactosidase; cheese whey; lactose-hydrolysis; biocatalyst. |
title_short |
Cell permeabilization of Kluyveromyces and Saccharomyces species to obtain potential biocatalysts for lactose hydrolysis |
title_full |
Cell permeabilization of Kluyveromyces and Saccharomyces species to obtain potential biocatalysts for lactose hydrolysis |
title_fullStr |
Cell permeabilization of Kluyveromyces and Saccharomyces species to obtain potential biocatalysts for lactose hydrolysis |
title_full_unstemmed |
Cell permeabilization of Kluyveromyces and Saccharomyces species to obtain potential biocatalysts for lactose hydrolysis |
title_sort |
Cell permeabilization of Kluyveromyces and Saccharomyces species to obtain potential biocatalysts for lactose hydrolysis |
author |
Alves, Érika de Pádua |
author_facet |
Alves, Érika de Pádua Bosso, Alessandra Morioka, Luiz Rodrigo Ito Suguimoto, Hélio Hiroshi |
author_role |
author |
author2 |
Bosso, Alessandra Morioka, Luiz Rodrigo Ito Suguimoto, Hélio Hiroshi |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Alves, Érika de Pádua Bosso, Alessandra Morioka, Luiz Rodrigo Ito Suguimoto, Hélio Hiroshi |
dc.subject.por.fl_str_mv |
beta-galactosidase; cheese whey; lactose-hydrolysis; biocatalyst. beta-galactosidase; cheese whey; lactose-hydrolysis; biocatalyst. |
topic |
beta-galactosidase; cheese whey; lactose-hydrolysis; biocatalyst. beta-galactosidase; cheese whey; lactose-hydrolysis; biocatalyst. |
description |
Yeast’s beta-galactosidase is an intracellular enzyme, through which it is possible to determine in vivo its activity as a biocatalyst in the lactose hydrolysis. Permeabilization process was used for transforming the microorganisms cells into biocatalysts with an enhanced enzyme activity. The potential application of this enzyme technology in industrial process depends mainly on the enzyme activity. Beta-galactosidase enzyme that hydrolyzes lactose, for instance, is largely dependent on the reaction time and its stability under different physical conditions, such as pH, temperature and enzyme concentration. The objective of this study was to optimize the cellular permeabilization process of Kluyveromyces marxianus CCT 3172 and Saccharomyces fragilis CCT 7586 cultured in cheese whey for lactose hydrolysis. Box-Behnken design was carried out for cell permeabilization with three independent variables, ethanol concentration, permeabilization time and temperature. The best permeability conditions for K. marxianus CCT 3172 were 27% (v v-1) ethanol, 3 min at 20ºC, with specific enzymatic activity of 0.98 U mg-1. For S. fragilis CCT 7586, a specific enzymatic activity of 1.31 U mg-1 was achieved using 45% (v v-1) of ethanol, 17 min. of reaction under 17ºC. Thus, it was concluded that cellular permeabilization with ethanol is an efficient process to determine beta-galactosidase activity. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-05-18 |
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/60336 10.4025/actascibiolsci.v44i1.60336 |
url |
http://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSci/article/view/60336 |
identifier_str_mv |
10.4025/actascibiolsci.v44i1.60336 |
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/60336/751375154205 |
dc.rights.driver.fl_str_mv |
Copyright (c) 2022 Acta Scientiarum. Biological Sciences http://creativecommons.org/licenses/by/4.0 info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
Copyright (c) 2022 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 44 (2022): Publicação contínua; e60336 Acta Scientiarum. Biological Sciences; v. 44 (2022): Publicação contínua; e60336 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 |
_version_ |
1799317391383986176 |