Nitrogen source and pH interact and modulate lipase secretion in a non-clinical strain of Candida parapsilosis

Detalhes bibliográficos
Autor(a) principal: Ribas, Rodolfo Kruger da Camara
Data de Publicação: 2019
Outros Autores: Carboni, Diorgenes dos Santos, Cazarolli, Juciana Clarice, Flôres, Simone Hickmann, Ramírez Castrillón, Mauricio, Silva, Patrícia Valente da
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.
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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
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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
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dc.language.iso.fl_str_mv eng
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dc.relation.ispartof.pt_BR.fl_str_mv Acta Scientiarum : Biological Sciences. Maringá. Vol. 41 (2019), e45481, 12 p.
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