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

Abstract

In this study, lipase from Candida antarctica B (Lipozyme CaLB-L) was successfully immobilized on SiO 2 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 SiO 2 was found to be a good catalyst and, under optimal conditions, esters could be obtained with conversion 44%, enantiomeric excess of product (ee p ) > 99%, enantiomeric excess of substract (ee s ) 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.

Superparamagnetic iron oxide nanoparticles (SPIONs) conjugated with lipase Candida antarctica A for biodiesel synthesis

“…However, other supporting materials such as silica, carbon, alumina and polymer nanoparticles, have also been used for preparation of nano catalysts for specic applications conferring greater structural rigidity 12 and stability to the biomolecules, 13,14 while keeping the enzymatic activity. 15 Additional advantages such as improved activity and selectivity, reduced inhibition, as well as ease recovery and reuse of biological material [16][17][18][19] upon immobilization have been reported.…”

Convenient enzymatic resolution of (R,S)‐2‐methylbutyric acid catalyzed by immobilized lipases

“…The reuse of lipases immobilized on SiO 2 has been previously described for our group . Here, we evaluated as well the reuse of ROL immobilized on sugarcane bagasse.…”

“…The dry bagasse was placed in an Erlenmeyer flask (1 g) along with phosphate buffer (100 mL) (Na 2 HPO 4 /KH 2 PO 4 0.07 mol L −1 ; pH 7.2) and the lipase, that is, CRL, MJL, or ROL (200 mg). The mixture was shaken (150 rpm) at 35°C (optimal temperature of most lipases herein used) for 2 h. Lipozyme CaLB‐L and lipase from Thermomyces lanuginosus were immobilized onto SiO 2 according to Mittersteiner et al…”

“…In order to confirm the selectivity, (R)-pentyl 2methylbutyrate catalyzed by CaLB was isolated by column chromatography (eluent: hexane and AcOEt 90: The reuse of lipases immobilized on SiO 2 has been previously described for our group. 28 Here, we evaluated as well the reuse of ROL immobilized on sugarcane bagasse. We observed the results for four consecutive reactions in the preparation of (S)-pentyl 2methylbutyrate ( Figure 2).…”

Microbial lipases and their industrial applications: a comprehensive review

“…The molecule chirality lies in the 1-methoxy-2-aminopropane part of the structure in the case of dimethenamid [ 430 ]. Without addition of organic solvent using neat reagents the reaction takes place at 20–60 °C and accomplishes transformations of > 60% with (S)-amine ee > 99% using immobilized CalB (Novozym 435 or L2 from Chirazyme), however the undesirable (R)- amide is reprocessed further [ 431 ]. Due to the extraction or distillation process the undesirable (R)-amide and alcohol by-product can be upgraded the desired (S)-amine.…”