title: Interfacial activation of lipases on hydrophobic support and application in the synthesis of a lubricant ester.
abstract: n-Octyl oleate was synthetized by enzymatic esterification reaction of oleic acid and n-octanol. Lipases from porcine pancreatic (PPL), Mucor javanicus (MJL), Candida sp. (CALA), Rhizomucor miehei (RML) and Thermomyces lanuginosus (TLL) were immobilized via interfacial activation on poly-methacrylate particles (PMA) and tested as biocatalysts. Their catalytic properties were determined in the hydrolysis of olive oil emulsion. Among them, TLL-PMA was the biocatalyst that yielded the highest hydrolytic activity (217.8±1.1 IU/g) and immobilized protein loading (37.5±0.4mg/g). This biocatalyst was also the most active in n-octyl oleate synthesis, thus selected for further studies. Maximum conversion percentage of 95.1±1.3% was observed after 60min of reaction at 45°C, 10% m/v of TLL-PMA, and molar ratio oleic acid:n-octanol of 1:1.5 in a solvent-free system. The biocatalyst fully retained its original activity after twelve cycles of reaction of 60min each. The product was confirmed by attenuated total reflectance Fourier transform infrared (ATR-FTIR) spectroscopy analysis and their physico-chemical properties were determined according to ASTM standard methods. These results show that the immobilization of an alkalophilic and thermostable lipase (TLL) on PMA particles allowed the preparation of a highly active biocatalyst in hydrolysis and esterification reactions.
authors.affiliation: Institute of Chemistry, Federal University of Alfenas, 37130-000, Alfenas, MG, Brazil.
authors.forename: Jaquelinne J
authors.initials: JJ
authors.lastname: Bassi
authors.affiliation: Institute of Chemistry, Federal University of Alfenas, 37130-000, Alfenas, MG, Brazil.
authors.forename: Larissa M
authors.initials: LM
authors.lastname: Todero
authors.affiliation: Institute of Chemistry, Federal University of Alfenas, 37130-000, Alfenas, MG, Brazil.
authors.forename: Flávia A P
authors.initials: FA
authors.lastname: Lage
authors.affiliation: Institute of Chemistry, Federal University of Alfenas, 37130-000, Alfenas, MG, Brazil.
authors.forename: Gabrielly I
authors.initials: GI
authors.lastname: Khedy
authors.affiliation: Institute of Chemistry, Federal University of Alfenas, 37130-000, Alfenas, MG, Brazil.
authors.forename: Jamile Dell
authors.initials: JD
authors.lastname: Ducas
authors.affiliation: Institute of Chemistry, Federal University of Alfenas, 37130-000, Alfenas, MG, Brazil.
authors.forename: Ana Paula
authors.initials: AP
authors.lastname: Custódio
authors.affiliation: Institute of Chemistry, Federal University of Alfenas, 37130-000, Alfenas, MG, Brazil.
authors.forename: Marilene A
authors.initials: MA
authors.lastname: Pinto
authors.affiliation: Institute of Chemistry, Federal University of Alfenas, 37130-000, Alfenas, MG, Brazil. Electronic address: adriano.mendes@unifal-mg.edu.br.
authors.forename: Adriano A
authors.initials: AA
authors.lastname: Mendes
mesh_terms: D000818:Animals; D055162:Biocatalysis / Q000187:drug effects; D004789:Enzyme Activation / Q000187:drug effects; D004795:Enzyme Stability / Q000187:drug effects; D004800:Enzymes, Immobilized / Q000378:metabolism; D004951:Esterification / Q000187:drug effects; D006868:Hydrolysis; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D054327:Lubricants / Q000494:pharmacology*; D019301:Oleic Acid / Q000378:metabolism; D011109:Polymethacrylic Acids / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared; D034421:Sus scrofa; D013696:Temperature
chemical_list: D004800:Enzymes, Immobilized; D054327:Lubricants; D011109:Polymethacrylic Acids; C030613:polymethacrylic acid; D019301:Oleic Acid; D008049:Lipase
keywords: Biolubricant synthesis; Hydrophobic support; Lipase immobilization