Application of lipase immobilized on a hydrophobic support for the synthesis of aromatic esters

dc.creatorSantos, Marta Maria Oliveira dos
dc.creatorGama, Rafaela Santos
dc.creatorTavares, Iasnaia Maria de Carvalho
dc.creatorSantos, Pedro Henrique
dc.creatorGonçalves, Márcia Soares
dc.creatorCarvalho, Marise Silva de
dc.creatorVilas Boas, Eduardo Valério de Barros
dc.creatorOliveira, Julieta Rangel de
dc.creatorMendes, Adriano Aguiar
dc.creatorFranco, Marcelo
dc.date.accessioned2021-07-08T16:32:51Z
dc.date.available2021-07-08T16:32:51Z
dc.date.issued2020-05
dc.description.abstractThe present study aimed at preparing three biocatalysts via physical adsorption of lipases from Candida rugosa (CRL), Mucor javanicus, and Candida sp. on a hydrophobic and mesoporous support (Diaion HP-20). These biocatalysts were later applied to the synthesis of aromatic esters of apple peel and citrus (hexyl butyrate), apple and rose (geranyl butyrate), and apricot and pineapple (propyl butyrate). Scanning electron microscopy and gel electrophoresis confirmed a selective adsorption of lipases on Diaion, thus endorsing simultaneous immobilization and purification. Gibbs free energy (∆G) evinced the spontaneity of the process (–17.9 kJ/mol ≤ ∆G ≤ –5.1 kJ/mol). Maximum immobilized protein concentration of 30 mg/g support by CRL. This biocatalyst was the most active in olive oil hydrolysis (hydrolytic activity of 126.0 ± 2.0 U/g) and in the synthesis of aromatic esters. Maximum conversion yield of 89.1% was attained after 150 Min for the synthesis of hexyl butyrate, followed by the synthesis of geranyl butyrate (87.3% after 240 Min) and propyl butyrate (80.0% after 150 Min). CRL immobilized on Diaion retained around 93% of its original activity after six consecutive cycles of 150 Min for the synthesis of hexyl butyrate.pt_BR
dc.identifier.citationSANTOS, M. M. O. dos et al. Application of lipase immobilized on a hydrophobic support for the synthesis of aromatic esters. Biotechnology and Applied Biochemistry, [S. I.], v. 68, n. 3, p. 538-546, Jun. 2021. DOI: https://doi.org/10.1002/bab.1959.pt_BR
dc.identifier.urihttps://repositorio.ufla.br/handle/1/46697
dc.identifier.urihttps://doi.org/10.1002/bab.1959pt_BR
dc.languageenpt_BR
dc.publisherInternational Union of Biochemistry and Molecular Biologypt_BR
dc.rightsrestrictAccesspt_BR
dc.sourceBiotechnology and Applied Biochemistrypt_BR
dc.subjectBiocatalysispt_BR
dc.subjectLipase immobilizationpt_BR
dc.subjectAroma synthesispt_BR
dc.subjectBiocatálisept_BR
dc.subjectImobilização de lipasept_BR
dc.subjectSíntese de ésteres de aromaspt_BR
dc.titleApplication of lipase immobilized on a hydrophobic support for the synthesis of aromatic esterspt_BR
dc.typeArtigopt_BR

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