Biotechnological valorization of mycelium-bound lipase of Penicillium purpurogenum in hydrolysis of high content lauric acid vegetable oils

Detalhes bibliográficos
Autor(a) principal: de Castro, Tarsila F.
Data de Publicação: 2022
Outros Autores: 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.
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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spelling 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