Nitrogen source and pH interact and modulate lipase secretion in a non-clinical strain of Candida parapsilosis
Autor(a) principal: | |
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Data de Publicação: | 2019 |
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/45481 |
Resumo: | Lipases (E.C. 3.1.1.3) are serine-hydrolases, and act on long chain fatty acid ester bonds. They exhibit specific and enantioselective activities, which are desirable for many industrial applications. This study aimed at screening and optimizing the production of lipases by wild yeast strains from a variety of substrates, as well as characterizing the enzyme. An initial selection was made in oxygenated oil-supplemented minimum medium, and the enzymatic activity of the supernatant was tested over p- nitrophenyl palmitate. One-hundred and twenty-four yeast strains from different substrates were tested, and twenty-three showed significantly higher lipolytic activity (p <0.01). One yeast in particular, QU110, showed best lipase production and therefore was selected for the optimization and characterization processes. This yeast exhibits enzyme secretion in initial pH 6.0, with olive oil and tryptone as carbon and nitrogen sources, respectively. There was a strong interaction between nitrogen source and initial pH, and pH 9.0 seems to inhibit enzyme secretion. The crude enzyme (cell-free supernatant) shows stability in surfactants and n-hexane, but not in ethanol or methanol. A Response Surface Model was created and optimal enzyme activity conditions were observed at 36°C and pH 8.0. The lipase is appropriate for transesterification reactions, as the enzyme is more stable in strong apolar solvents than moderately apolar ones. Also, secretion by pH was not reported elsewhere, which should be further investigated and contribute for other yeast bioprocesses as well. |
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Nitrogen source and pH interact and modulate lipase secretion in a non-clinical strain of Candida parapsilosisp-NPPtryptoneyeastpalmitateResponse Surface Modelserine-hydrolaseLipases (E.C. 3.1.1.3) are serine-hydrolases, and act on long chain fatty acid ester bonds. They exhibit specific and enantioselective activities, which are desirable for many industrial applications. This study aimed at screening and optimizing the production of lipases by wild yeast strains from a variety of substrates, as well as characterizing the enzyme. An initial selection was made in oxygenated oil-supplemented minimum medium, and the enzymatic activity of the supernatant was tested over p- nitrophenyl palmitate. One-hundred and twenty-four yeast strains from different substrates were tested, and twenty-three showed significantly higher lipolytic activity (p <0.01). One yeast in particular, QU110, showed best lipase production and therefore was selected for the optimization and characterization processes. This yeast exhibits enzyme secretion in initial pH 6.0, with olive oil and tryptone as carbon and nitrogen sources, respectively. There was a strong interaction between nitrogen source and initial pH, and pH 9.0 seems to inhibit enzyme secretion. The crude enzyme (cell-free supernatant) shows stability in surfactants and n-hexane, but not in ethanol or methanol. A Response Surface Model was created and optimal enzyme activity conditions were observed at 36°C and pH 8.0. The lipase is appropriate for transesterification reactions, as the enzyme is more stable in strong apolar solvents than moderately apolar ones. Also, secretion by pH was not reported elsewhere, which should be further investigated and contribute for other yeast bioprocesses as well.Universidade Estadual De Maringá2019-12-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSci/article/view/4548110.4025/actascibiolsci.v41i1.45481Acta Scientiarum. Biological Sciences; Vol 41 (2019): Publicação contínua; e45481Acta Scientiarum. Biological Sciences; v. 41 (2019): Publicação contínua; e454811807-863X1679-9283reponame:Acta Scientiarum Biological Sciencesinstname:Universidade Estadual de Maringá (UEM)instacron:UEMenghttp://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSci/article/view/45481/751375149047Copyright (c) 2019 Acta Scientiarum. Biological Scienceshttps://creativecommons.org/licenses/by/4.0info:eu-repo/semantics/openAccessRibas, Rodolfo Krüger da CâmaraCarboni, Diórgenes dos SantosCazarolli, Juciana ClariceFlôres, Simone HickmannRamirez-Castrillon, MaurícioValente, Patricia2022-02-20T21:59:12Zoai:periodicos.uem.br/ojs:article/45481Revistahttp://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSciPUBhttp://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSci/oai||actabiol@uem.br1807-863X1679-9283opendoar:2022-02-20T21:59:12Acta Scientiarum Biological Sciences - Universidade Estadual de Maringá (UEM)false |
dc.title.none.fl_str_mv |
Nitrogen source and pH interact and modulate lipase secretion in a non-clinical strain of Candida parapsilosis |
title |
Nitrogen source and pH interact and modulate lipase secretion in a non-clinical strain of Candida parapsilosis |
spellingShingle |
Nitrogen source and pH interact and modulate lipase secretion in a non-clinical strain of Candida parapsilosis Ribas, Rodolfo Krüger da Câmara p-NPP tryptone yeast palmitate Response Surface Model serine-hydrolase |
title_short |
Nitrogen source and pH interact and modulate lipase secretion in a non-clinical strain of Candida parapsilosis |
title_full |
Nitrogen source and pH interact and modulate lipase secretion in a non-clinical strain of Candida parapsilosis |
title_fullStr |
Nitrogen source and pH interact and modulate lipase secretion in a non-clinical strain of Candida parapsilosis |
title_full_unstemmed |
Nitrogen source and pH interact and modulate lipase secretion in a non-clinical strain of Candida parapsilosis |
title_sort |
Nitrogen source and pH interact and modulate lipase secretion in a non-clinical strain of Candida parapsilosis |
author |
Ribas, Rodolfo Krüger da Câmara |
author_facet |
Ribas, Rodolfo Krüger da Câmara Carboni, Diórgenes dos Santos Cazarolli, Juciana Clarice Flôres, Simone Hickmann Ramirez-Castrillon, Maurício Valente, Patricia |
author_role |
author |
author2 |
Carboni, Diórgenes dos Santos Cazarolli, Juciana Clarice Flôres, Simone Hickmann Ramirez-Castrillon, Maurício Valente, Patricia |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Ribas, Rodolfo Krüger da Câmara Carboni, Diórgenes dos Santos Cazarolli, Juciana Clarice Flôres, Simone Hickmann Ramirez-Castrillon, Maurício Valente, Patricia |
dc.subject.por.fl_str_mv |
p-NPP tryptone yeast palmitate Response Surface Model serine-hydrolase |
topic |
p-NPP tryptone yeast palmitate Response Surface Model serine-hydrolase |
description |
Lipases (E.C. 3.1.1.3) are serine-hydrolases, and act on long chain fatty acid ester bonds. They exhibit specific and enantioselective activities, which are desirable for many industrial applications. This study aimed at screening and optimizing the production of lipases by wild yeast strains from a variety of substrates, as well as characterizing the enzyme. An initial selection was made in oxygenated oil-supplemented minimum medium, and the enzymatic activity of the supernatant was tested over p- nitrophenyl palmitate. One-hundred and twenty-four yeast strains from different substrates were tested, and twenty-three showed significantly higher lipolytic activity (p <0.01). One yeast in particular, QU110, showed best lipase production and therefore was selected for the optimization and characterization processes. This yeast exhibits enzyme secretion in initial pH 6.0, with olive oil and tryptone as carbon and nitrogen sources, respectively. There was a strong interaction between nitrogen source and initial pH, and pH 9.0 seems to inhibit enzyme secretion. The crude enzyme (cell-free supernatant) shows stability in surfactants and n-hexane, but not in ethanol or methanol. A Response Surface Model was created and optimal enzyme activity conditions were observed at 36°C and pH 8.0. The lipase is appropriate for transesterification reactions, as the enzyme is more stable in strong apolar solvents than moderately apolar ones. Also, secretion by pH was not reported elsewhere, which should be further investigated and contribute for other yeast bioprocesses as well. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-12-06 |
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/45481 10.4025/actascibiolsci.v41i1.45481 |
url |
http://www.periodicos.uem.br/ojs/index.php/ActaSciBiolSci/article/view/45481 |
identifier_str_mv |
10.4025/actascibiolsci.v41i1.45481 |
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/45481/751375149047 |
dc.rights.driver.fl_str_mv |
Copyright (c) 2019 Acta Scientiarum. Biological Sciences https://creativecommons.org/licenses/by/4.0 info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
Copyright (c) 2019 Acta Scientiarum. Biological Sciences https://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 41 (2019): Publicação contínua; e45481 Acta Scientiarum. Biological Sciences; v. 41 (2019): Publicação contínua; e45481 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_ |
1799317397388132352 |