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PublicationJournal of Molecular Catalysis B: Enzymatic

Evaluation of different immobilized lipases in transesterification reactions using tributyrin: Advantages of the heterofunctional octyl agarose beads

Authors:Roberto Fernandez-Lafuente
Groups of research:Optimization of biocatalysts and bioprocesses
Daniela B. Hirata1,2, Tiago L. Albuquerque1,3, Nazzoly Rueda1,4, Jose J. Virgen-Ortíz1, Veymar G. Tacias-Pascacio1,5, Roberto Fernandez-Lafuente1,*
1. Departamento de Biocatálisis, Instituto de Catálisis-CSIC, Campus UAM-CSIC, Cantoblanco, 28049 Madrid, Spain.
2. Instituto de Química, Universidade Federal de Alfenas, 37130-000 Alfenas, MG, Brazil.
3. Departamento de Engenharia Química, Universidade Federal Do Ceará, Campus Do Pici, CEP 60455-760, Fortaleza, CE, Brazil.
4. Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga, Colombia.
5. Unidad de Investigación y Desarrollo en Alimentos. Instituto Tecnológico de Veracruz, Calzada Miguel A. de Quevedo 2779, 91897 Veracruz, Mexico.

Lipases from Candida antarctica (A and B) (CALA and CALB), Candida rugosa (CRL), Thermomyces lanuginosus (TLL) and Rhizomucor miehei (RML), as well as the chimeric phospholipase Lecitase Ultra (LU) were immobilized on octyl agarose or on heterofunctional octyl supports. RML, CRL and TLL were covalently immobilized on octyl agarose beads activated with divinyl sulfone (OCDVS), while the other lipases were immobilized on octyl-glyoxyl beads (OCGLX). The 12 biocatalysts were utilized in the production of esters using tributyrin and 20% (v/v) methanol, ethanol or isopropanol via a kinetically controlled strategy. All preparations produced the desired ester, except RML, TLL and LU for isopropyl butyrate. CALA showed the best performance in these reactions, with maximum yields over 40%. The immobilization on heterofunctional supports usually reduced the activity and even the maximum yields, although some exceptions were relevant (e.g., CALA or CALB in the production of ethyl butyrate). The effect of the nucleophile was also very different using the just physically adsorbed or the covalently immobilized preparations, some instances one preparation have as best substrate an alcohol while the best substrate was other alcohol using the other lipase preparation.
            Using CALB as model enzyme, we have shown the advantages of the use of the covalent preparation. The increase of the alcohol permitted the increase in maximum ester yields. However, the combined presence of dibutyrin and alcohol prevented the reuse of OC-CALB due to the enzyme desorption, while the covalent preparation could be reused by 6 cycles
Keywords:heterofunctional supports, Lipase immobilization, interfacial activation, transesterification, enzyme release
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