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

Publication date: Available online 11 August 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Daniela B. Hirata, Tiago L. Albuquerque, Nazzoly Rueda, Jose J. Virgen-Ortíz, Veymar G. Tacias-Pascacio, Roberto Fernandez-Lafuente 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 o...
Source: Journal of Molecular Catalysis B: Enzymatic - Category: Biochemistry Source Type: research