Immobilization of CALB on activated chitosan: Application to enzymatic synthesis in supercritical and near-critical carbon dioxide

Autor: José C.S. dos Santos, Horacio L. Bonazza, Leonardo J.B.L. de Matos, Elizabete A. Carneiro, Oveimar Barbosa, Roberto Fernandez-Lafuente, Luciana R.B. Gonçalves, Hosiberto B. de Sant’ Ana, Rílvia S. Santiago-Aguiar
Jazyk: angličtina
Rok vydání: 2017
Předmět:
Zdroj: Biotechnology Reports, Vol 14, Iss C, Pp 16-26 (2017)
Druh dokumentu: article
ISSN: 2215-017X
DOI: 10.1016/j.btre.2017.02.003
Popis: The objective of this new paper was to evaluate the enzymatic esterification reaction conducted in supercritical or near-critical CO2, catalyzed by immobilized lipase B from Candida antarctica (CALB). The biocatalyst was prepared through the immobilization of CALB by covalent attachment using chitosan sequentially activated with Glycidol, ethylenediamine (EDA) and glutaraldehyde as support. In order to determine the best operational conditions of the esterification reaction (1: 1 (alcohol–acid); biocatalyst content, 10% (by substrate mass); 45 °C), an experimental design (23) was conducted to evaluate the effects of the following parameters: alcohol to oil molar ratios, reaction time and temperature. The maximum loading of chitosan was 20 mg protein/g support, and the thermal and solvent stability of the new biocatalyst was higher than that of the CALB-GX (by a 26-fold factor), CALB-OC (by a 53-fold factor) and Novozym 435 (by a 3-fold factor). The maximum conversion was 46.9% at a temperature of 29.9 °C, ethanol to oleic acid molar ratio equal to 4.50:1, and a reaction time of 6.5 h. Additionally, the removal of water from the medium, by using molecular sieves, promoted a 16.0% increase in the conversion of oleic acid into ethyl esters.
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