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

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 an...

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Bibliographic Details
Published in:Journal of the Brazilian Chemical Society 2017-07, Vol.28 (7), p.1185-1192
Main Authors: Mittersteiner, Mateus, Machado, Tayani, de Jesus, Paulo Cesar, Brondani, Patrícia, Scharf, Dilamara, Wendhausen Jr, Renato
Format: Article
Language:English
Subjects:
CHEMISTRY, MULTIDISCIPLINARY
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Summary: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.
ISSN:0103-5053
1678-4790
DOI:10.21577/0103-5053.20160277