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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Bassi, Jaquelinne J. Todero, Larissa M. Lage, Flávia A. P. Khedy, Gabrielly I. Ducas, Jamile Dell Custódio, Ana Paula Pinto, Marilene A. Mendes, Adriano A. |
| Description | Country affiliation: Brazil Author Affiliation: Bassi JJ ( Institute of Chemistry, Federal University of Alfenas, 37130-000, Alfenas, MG, Brazil.); Todero LM ( Institute of Chemistry, Federal University of Alfenas, 37130-000, Alfenas, MG, Brazil.); Lage FA ( Institute of Chemistry, Federal University of Alfenas, 37130-000, Alfenas, MG, Brazil.); Khedy GI ( Institute of Chemistry, Federal University of Alfenas, 37130-000, Alfenas, MG, Brazil.); Ducas JD ( Institute of Chemistry, Federal University of Alfenas, 37130-000, Alfenas, MG, Brazil.); Custódio AP ( Institute of Chemistry, Federal University of Alfenas, 37130-000, Alfenas, MG, Brazil.); Pinto MA ( Institute of Chemistry, Federal University of Alfenas, 37130-000, Alfenas, MG, Brazil.); Mendes AA ( Institute of Chemistry, Federal University of Alfenas, 37130-000, Alfenas, MG, Brazil. Electronic address: adriano.mendes@unifal-mg.edu.br.) |
| 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. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| Journal | International Journal of Biological Macromolecules |
| Volume Number | 92 |
| e-ISSN | 18790003 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2016-11-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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