Litcius/Paper detail

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

Marta Maria Oliveira dos Santos, Rafaela S. Gama, Iasnaia Maria de Carvalho Tavares, Pedro Henrique Santos, Márcia Soares Gonçalves, Marise Silva de Carvalho, Eduardo Valério de Barros Vilas Boas, Julieta Rangel de Oliveira, Adriano A. Méndes, Marcelo Franco

2020Biotechnology and Applied Biochemistry28 citationsDOI

Abstract

The 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.

Topics & Concepts

ChemistryCandida rugosaLipaseButyrateHydrolysisRhizopus oryzaeOrganic chemistryBiocatalysisAdsorptionChromatographyTriacylglycerol lipaseNuclear chemistryFermentationCatalysisEnzymeIonic liquidEnzyme Catalysis and ImmobilizationElectrochemical sensors and biosensorsMicrobial Metabolic Engineering and Bioproduction