Nitrogen source and pH interact and modulate lipase secretion in a non-clinical strain of Candida parapsilosis
Autor(a) principal: | |
---|---|
Data de Publicação: | 2019 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UFRGS |
Texto Completo: | http://hdl.handle.net/10183/218519 |
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. |
id |
UFRGS-2_6126215a83ef5643f74d419a5bf3f72e |
---|---|
oai_identifier_str |
oai:www.lume.ufrgs.br:10183/218519 |
network_acronym_str |
UFRGS-2 |
network_name_str |
Repositório Institucional da UFRGS |
repository_id_str |
|
spelling |
Ribas, Rodolfo Kruger da CamaraCarboni, Diorgenes dos SantosCazarolli, Juciana ClariceFlôres, Simone HickmannRamírez Castrillón, MauricioSilva, Patrícia Valente da2021-03-09T04:53:14Z20191807-863Xhttp://hdl.handle.net/10183/218519001122352Lipases (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.application/pdfengActa Scientiarum : Biological Sciences. Maringá. Vol. 41 (2019), e45481, 12 p.LipaseCandida parapsilosisLevedurasNitrogênioP-NPPTryptoneYeastPalmitateResponse surface modelSerine-hydrolaseNitrogen source and pH interact and modulate lipase secretion in a non-clinical strain of Candida parapsilosisinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/otherinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UFRGSinstname:Universidade Federal do Rio Grande do Sul (UFRGS)instacron:UFRGSTEXT001122352.pdf.txt001122352.pdf.txtExtracted Texttext/plain32347http://www.lume.ufrgs.br/bitstream/10183/218519/2/001122352.pdf.txt9e95f4eef68f385a70223f5f977687dfMD52ORIGINAL001122352.pdfTexto completo (inglês)application/pdf1014711http://www.lume.ufrgs.br/bitstream/10183/218519/1/001122352.pdf9bdc20808580080b1e349f95e22fc9d0MD5110183/2185192021-05-07 05:14:24.705866oai:www.lume.ufrgs.br:10183/218519Repositório de PublicaçõesPUBhttps://lume.ufrgs.br/oai/requestopendoar:2021-05-07T08:14:24Repositório Institucional da UFRGS - Universidade Federal do Rio Grande do Sul (UFRGS)false |
dc.title.pt_BR.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 Kruger da Camara Lipase Candida parapsilosis Leveduras Nitrogênio 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 Kruger da Camara |
author_facet |
Ribas, Rodolfo Kruger da Camara Carboni, Diorgenes dos Santos Cazarolli, Juciana Clarice Flôres, Simone Hickmann Ramírez Castrillón, Mauricio Silva, Patrícia Valente da |
author_role |
author |
author2 |
Carboni, Diorgenes dos Santos Cazarolli, Juciana Clarice Flôres, Simone Hickmann Ramírez Castrillón, Mauricio Silva, Patrícia Valente da |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Ribas, Rodolfo Kruger da Camara Carboni, Diorgenes dos Santos Cazarolli, Juciana Clarice Flôres, Simone Hickmann Ramírez Castrillón, Mauricio Silva, Patrícia Valente da |
dc.subject.por.fl_str_mv |
Lipase Candida parapsilosis Leveduras Nitrogênio |
topic |
Lipase Candida parapsilosis Leveduras Nitrogênio P-NPP Tryptone Yeast Palmitate Response surface model Serine-hydrolase |
dc.subject.eng.fl_str_mv |
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.issued.fl_str_mv |
2019 |
dc.date.accessioned.fl_str_mv |
2021-03-09T04:53:14Z |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/other |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10183/218519 |
dc.identifier.issn.pt_BR.fl_str_mv |
1807-863X |
dc.identifier.nrb.pt_BR.fl_str_mv |
001122352 |
identifier_str_mv |
1807-863X 001122352 |
url |
http://hdl.handle.net/10183/218519 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.pt_BR.fl_str_mv |
Acta Scientiarum : Biological Sciences. Maringá. Vol. 41 (2019), e45481, 12 p. |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UFRGS instname:Universidade Federal do Rio Grande do Sul (UFRGS) instacron:UFRGS |
instname_str |
Universidade Federal do Rio Grande do Sul (UFRGS) |
instacron_str |
UFRGS |
institution |
UFRGS |
reponame_str |
Repositório Institucional da UFRGS |
collection |
Repositório Institucional da UFRGS |
bitstream.url.fl_str_mv |
http://www.lume.ufrgs.br/bitstream/10183/218519/2/001122352.pdf.txt http://www.lume.ufrgs.br/bitstream/10183/218519/1/001122352.pdf |
bitstream.checksum.fl_str_mv |
9e95f4eef68f385a70223f5f977687df 9bdc20808580080b1e349f95e22fc9d0 |
bitstream.checksumAlgorithm.fl_str_mv |
MD5 MD5 |
repository.name.fl_str_mv |
Repositório Institucional da UFRGS - Universidade Federal do Rio Grande do Sul (UFRGS) |
repository.mail.fl_str_mv |
|
_version_ |
1801225009523326976 |