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
Main Authors: Mittersteiner,Mateus, Machado,Tayani M., Jesus,Paulo Cesar de, Brondani,Patrícia B., Scharf,Dilamara R., Wendhausen Jr.,Renato
Format: Article in Journal/Newspaper
Language:English
Published: Sociedade Brasileira de Química 2017
Subjects:
lipases
immobilization
silica gel
enzymatic resolution
acylation reactions
Antarc*
Antarctica
Online Access:http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532017000701185
Description
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.

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