Biotechnological valorization of mycelium-bound lipase of Penicillium purpurogenum in hydrolysis of high content lauric acid vegetable oils
Autor(a) principal: | |
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Data de Publicação: | 2022 |
Outros Autores: | , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1016/j.psep.2022.03.013 http://hdl.handle.net/11449/223719 |
Resumo: | The study deals with the direct use of whole cells of a species of Penicillium as biocatalyst (mycelium-bound lipase) for the hydrolysis of vegetable oils under low-power ultrasonic irradiation. Whole cells of Penicillium purpurogenum with lauric acid-specificity lipase were able to hydrolyze vegetable oils with high content of this fatty acid. Up to 90% hydrolysis values were reached at 7 h of reaction, providing high fatty acid contents in shorter times concerning the literature. The results suggest that the ultrasound wave improves the interfacial area and that the lipase of Penicillium purpurogenum is bound to the cell, in a place with easy access to the substrate. On the other hand, the presence in the substrate of fatty acids with 18 carbons (stearic, oleic, and linoleic) in a concentration greater than 20%, negatively interferes with the degree of hydrolysis, indicating a possible limitation of lipase specificity. The present study highlights the biotechnological potential of mycelium-bound lipase (naturally immobilized enzymes) for use in the hydrolysis of babassu, coconut and kernel oils, which are not directly integrated into the food production chain. |
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Biotechnological valorization of mycelium-bound lipase of Penicillium purpurogenum in hydrolysis of high content lauric acid vegetable oilsBiomass valorizationHydrolysisLauric acidMycelium-bound lipasePenicillium purpurogenumThe study deals with the direct use of whole cells of a species of Penicillium as biocatalyst (mycelium-bound lipase) for the hydrolysis of vegetable oils under low-power ultrasonic irradiation. Whole cells of Penicillium purpurogenum with lauric acid-specificity lipase were able to hydrolyze vegetable oils with high content of this fatty acid. Up to 90% hydrolysis values were reached at 7 h of reaction, providing high fatty acid contents in shorter times concerning the literature. The results suggest that the ultrasound wave improves the interfacial area and that the lipase of Penicillium purpurogenum is bound to the cell, in a place with easy access to the substrate. On the other hand, the presence in the substrate of fatty acids with 18 carbons (stearic, oleic, and linoleic) in a concentration greater than 20%, negatively interferes with the degree of hydrolysis, indicating a possible limitation of lipase specificity. The present study highlights the biotechnological potential of mycelium-bound lipase (naturally immobilized enzymes) for use in the hydrolysis of babassu, coconut and kernel oils, which are not directly integrated into the food production chain.Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Department of Chemical Engineering School of Engineering of Lorena University of São Paulo, SPBiotechnological Processes and Macromolecules Purification Laboratory Federal University of São João del-Rei, MGDepartment of Bioprocess Engineering and Biotechnology Faculty of Pharmaceutical Sciences São Paulo State University, SPPostgraduate Program in Biotechnology Institute of Chemistry Federal University of Alfenas, MGFaculty of Pharmaceutical Sciences University of São Paulo, SPDepartment of Material Science University Center of Volta Redonda, RJDepartment of Bioprocess Engineering and Biotechnology Faculty of Pharmaceutical Sciences São Paulo State University, SPCAPES: 001FAPESP: 2020/15513-7Universidade de São Paulo (USP)Federal University of São João del-ReiUniversidade Estadual Paulista (UNESP)Federal University of AlfenasUniversity Center of Volta Redondade Castro, Tarsila F.Cortez, Daniela V.Gonçalves, Daniel B.Bento, Heitor B.S. [UNESP]Gonçalves, Rhyan L.N.Costa-Silva, Tales A.Gambarato, Bruno C.de Castro, Heizir F.de Carvalho, Ana Karine F.2022-04-28T19:52:41Z2022-04-28T19:52:41Z2022-05-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article498-505http://dx.doi.org/10.1016/j.psep.2022.03.013Process Safety and Environmental Protection, v. 161, p. 498-505.0957-5820http://hdl.handle.net/11449/22371910.1016/j.psep.2022.03.0132-s2.0-85127112158Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengProcess Safety and Environmental Protectioninfo:eu-repo/semantics/openAccess2022-04-28T19:52:42Zoai:repositorio.unesp.br:11449/223719Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T18:35:47.399275Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Biotechnological valorization of mycelium-bound lipase of Penicillium purpurogenum in hydrolysis of high content lauric acid vegetable oils |
title |
Biotechnological valorization of mycelium-bound lipase of Penicillium purpurogenum in hydrolysis of high content lauric acid vegetable oils |
spellingShingle |
Biotechnological valorization of mycelium-bound lipase of Penicillium purpurogenum in hydrolysis of high content lauric acid vegetable oils de Castro, Tarsila F. Biomass valorization Hydrolysis Lauric acid Mycelium-bound lipase Penicillium purpurogenum |
title_short |
Biotechnological valorization of mycelium-bound lipase of Penicillium purpurogenum in hydrolysis of high content lauric acid vegetable oils |
title_full |
Biotechnological valorization of mycelium-bound lipase of Penicillium purpurogenum in hydrolysis of high content lauric acid vegetable oils |
title_fullStr |
Biotechnological valorization of mycelium-bound lipase of Penicillium purpurogenum in hydrolysis of high content lauric acid vegetable oils |
title_full_unstemmed |
Biotechnological valorization of mycelium-bound lipase of Penicillium purpurogenum in hydrolysis of high content lauric acid vegetable oils |
title_sort |
Biotechnological valorization of mycelium-bound lipase of Penicillium purpurogenum in hydrolysis of high content lauric acid vegetable oils |
author |
de Castro, Tarsila F. |
author_facet |
de Castro, Tarsila F. Cortez, Daniela V. Gonçalves, Daniel B. Bento, Heitor B.S. [UNESP] Gonçalves, Rhyan L.N. Costa-Silva, Tales A. Gambarato, Bruno C. de Castro, Heizir F. de Carvalho, Ana Karine F. |
author_role |
author |
author2 |
Cortez, Daniela V. Gonçalves, Daniel B. Bento, Heitor B.S. [UNESP] Gonçalves, Rhyan L.N. Costa-Silva, Tales A. Gambarato, Bruno C. de Castro, Heizir F. de Carvalho, Ana Karine F. |
author2_role |
author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade de São Paulo (USP) Federal University of São João del-Rei Universidade Estadual Paulista (UNESP) Federal University of Alfenas University Center of Volta Redonda |
dc.contributor.author.fl_str_mv |
de Castro, Tarsila F. Cortez, Daniela V. Gonçalves, Daniel B. Bento, Heitor B.S. [UNESP] Gonçalves, Rhyan L.N. Costa-Silva, Tales A. Gambarato, Bruno C. de Castro, Heizir F. de Carvalho, Ana Karine F. |
dc.subject.por.fl_str_mv |
Biomass valorization Hydrolysis Lauric acid Mycelium-bound lipase Penicillium purpurogenum |
topic |
Biomass valorization Hydrolysis Lauric acid Mycelium-bound lipase Penicillium purpurogenum |
description |
The study deals with the direct use of whole cells of a species of Penicillium as biocatalyst (mycelium-bound lipase) for the hydrolysis of vegetable oils under low-power ultrasonic irradiation. Whole cells of Penicillium purpurogenum with lauric acid-specificity lipase were able to hydrolyze vegetable oils with high content of this fatty acid. Up to 90% hydrolysis values were reached at 7 h of reaction, providing high fatty acid contents in shorter times concerning the literature. The results suggest that the ultrasound wave improves the interfacial area and that the lipase of Penicillium purpurogenum is bound to the cell, in a place with easy access to the substrate. On the other hand, the presence in the substrate of fatty acids with 18 carbons (stearic, oleic, and linoleic) in a concentration greater than 20%, negatively interferes with the degree of hydrolysis, indicating a possible limitation of lipase specificity. The present study highlights the biotechnological potential of mycelium-bound lipase (naturally immobilized enzymes) for use in the hydrolysis of babassu, coconut and kernel oils, which are not directly integrated into the food production chain. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-04-28T19:52:41Z 2022-04-28T19:52:41Z 2022-05-01 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/j.psep.2022.03.013 Process Safety and Environmental Protection, v. 161, p. 498-505. 0957-5820 http://hdl.handle.net/11449/223719 10.1016/j.psep.2022.03.013 2-s2.0-85127112158 |
url |
http://dx.doi.org/10.1016/j.psep.2022.03.013 http://hdl.handle.net/11449/223719 |
identifier_str_mv |
Process Safety and Environmental Protection, v. 161, p. 498-505. 0957-5820 10.1016/j.psep.2022.03.013 2-s2.0-85127112158 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Process Safety and Environmental Protection |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
498-505 |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808128954211500032 |