Easy and Simple SiO2 Immobilization of Lipozyme CaLB-L: Its Use as a Catalyst in Acylation Reactions and Comparison with Other Lipases

AUTOR(ES)

Mittersteiner, Mateus, Machado, Tayani M., Jesus, Paulo Cesar de, Brondani, Patrícia B., Scharf, Dilamara R., Wendhausen Jr., Renato

FONTE

J. Braz. Chem. Soc.

DATA DE PUBLICAÇÃO

2017-07

RESUMO

In this study, lipase from Candida antarctica B (Lipozyme CaLB-L) was successfully immobilized on SiO2 through adsorption and used to obtain (R)-(+)-esters derived from (R,S)-1-phenylethanol. The new immobilized enzyme was compared with commercially immobilized lipases (Novozyme 435, Lipozyme 435 and Pseudomonas cepacia (PSC-II and PSD-I)). Lipozyme CaLB-L adsorbed onto SiO2 was found to be a good catalyst and, under optimal conditions, esters could be obtained with conversion 44%, enantiomeric excess of product (eep) > 99%, enantiomeric excess of substract (ees) 77% and enantiomeric ratio (E) > 200. The lipase maintained enantioselectivity under adverse conditions, such as in organic solvents, with an excess of substrate and at different temperatures. The immobilized lipase could be reused five times with no significant loss of the activity.

Documentos Relacionados

• A mild and simple iodination of phenols with trichloroisocyanuric acid/ I2 /Wet SiO2 system
• Modification of spherical SiO2 particles via electrolyte for high zeta potential and self-assembly of SiO2 photonic crystal
• Precipitation of amorphous SiO2 particles and their properties
• Formation of Aluminum Titanate with Small Additions of MgO and SiO2
• Comparative study of catalytic oxidation of ethanol to acetaldehyde using Fe(III) dispersed on Sb2O5 grafted on SiO2 and on untreated SiO2 surfaces