Free and Substrate-Immobilised Lipases from Fusarium verticillioides P24 as a Biocatalyst for Hydrolysis and Transesterification Reactions

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dc.contributor.authorBorges, Janaina Pires [UNESP]
dc.contributor.authorQuilles Junior, José Carlos [UNESP]
dc.contributor.authorOhe, Thiago Hideyuki Kobe [UNESP]
dc.contributor.authorFerrarezi, Ana Lucia [UNESP]
dc.contributor.authorNunes, Christiane da Costa Carreira [UNESP]
dc.contributor.authorBoscolo, Mauricio [UNESP]
dc.contributor.authorGomes, Eleni [UNESP]
dc.contributor.authorBocchini, Daniela Alonso [UNESP]
dc.contributor.authorda Silva, Roberto [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2020-12-12T02:19:27Z
dc.date.available2020-12-12T02:19:27Z
dc.date.issued2020-01-01
dc.description.abstractFungal enzymes are widely used in technological processes and have some interesting features to be applied in a variety of biosynthetic courses. Here, free and substrate-immobilised lipases from Fusarium verticillioides P24 were obtained by solid-state fermentation using wheat bran as substrate and fungal carrier. Based on their hydrolytic and transesterification activities, the lipases were characterised as pH-dependent in both reactions, with higher substrate conversion in an alkaline environment. Thermally, the lipases performed well from 30 to 45 °C, being more stable in mild conditions. Organic solvents significantly influenced the lipase selectivity using different vegetable oils as fatty acid source. Omega(ω)-3 production in n-hexane achieved 45% using canola oil, against ≈ 18% in cyclohexane. However, ω-6 production was preferably produced for both solvents using linseed oil with significant alterations in the yield (≈ 79% and 49% for n-hexane and cyclohexane, respectively). Moreover, the greatest enzyme selectivity for ω-6 led us to suppose a lipase preference for the Sn1 position of the triacylglycerol. Lastly, a transesterification reaction was performed, achieving 90% of ester conversion in 72 h. This study reports the characterisation and use of free and substrate-immobilised lipases from Fusarium verticillioides P24 as an economic and efficient method for the first time.en
dc.description.affiliationDepartament of Biochemistry and Chemical Technology IQ/UNESP, Rua Prof. Francisco Degni, 55, CEP
dc.description.affiliationDepartment of Chemistry and Environmental Sciences IBILCE/UNESP, Rua Cristóvão Colombo, 2265, CEP
dc.description.affiliationDepartment of Biology IBILCE/UNESP, Rua Cristóvão Colombo, 2265, CEP
dc.description.affiliationUnespDepartament of Biochemistry and Chemical Technology IQ/UNESP, Rua Prof. Francisco Degni, 55, CEP
dc.description.affiliationUnespDepartment of Chemistry and Environmental Sciences IBILCE/UNESP, Rua Cristóvão Colombo, 2265, CEP
dc.description.affiliationUnespDepartment of Biology IBILCE/UNESP, Rua Cristóvão Colombo, 2265, CEP
dc.identifierhttp://dx.doi.org/10.1007/s12010-020-03411-w
dc.identifier.citationApplied Biochemistry and Biotechnology.
dc.identifier.doi10.1007/s12010-020-03411-w
dc.identifier.issn1559-0291
dc.identifier.issn0273-2289
dc.identifier.scopus2-s2.0-85089545645
dc.identifier.urihttp://hdl.handle.net/11449/200914
dc.language.isoeng
dc.relation.ispartofApplied Biochemistry and Biotechnology
dc.sourceScopus
dc.subjectFusarium verticillioides
dc.subjectHydrolysis
dc.subjectLipase
dc.subjectOmega-3
dc.subjectOmega-6
dc.subjectTransesterification
dc.titleFree and Substrate-Immobilised Lipases from Fusarium verticillioides P24 as a Biocatalyst for Hydrolysis and Transesterification Reactionsen
dc.typeArtigo
unesp.author.orcid0000-0001-8877-4200[2]

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Artigos - Bioquímica e Tecnologia - IQ
Artigos - Biologia - IBILCE
Artigos - Química e Ciências Ambientais - IBILCE