Abstract
Lecitase™ Ultra was immobilized on four different supports and tested for the first time as the biocatalyst in the kinetic resolution of racemic allyl alcohols with the (E)-4-arylbut-3-en-2-ol system in the process of transesterification. The most effective biocatalyst turned out to be the enzyme immobilized on agarose activated with cyanogen bromide (LU-CNBr). The best results (E > 200, ees and eep = 95–99%) were obtained for (E)-4-phenylbut-3-en-2-ol and its analog with a 2,5-dimethylphenyl ring whereas the lowest ee of kinetic resolution products (90%) was achieved for the substrate with a 4-methoxyphenyl substituent. For all substrates, (R)-enantiomers were esterified faster than their (S)-antipodes. The results showed that LU-CNBr is a versatile biocatalyst, showing high activity and enantioselectivity in a wide range of organic solvents in the presence of commonly used acyl donors. High operational stability of LU-CNBr allows it to be reused in three subsequent reaction cycles without negative effects on the efficiency and enantioselectivity of transesterification. This biocatalyst can become attractive to the commercial lipases in the process of the kinetic resolution of allyl alcohols.
Highlights
Using enzymes as the biocatalysts of chemical reactions is a subject of interest for many researchers worldwide due to their wide spectrum of activity and high stereo- and regioselectivity [1,2,3].New environmental requirements concerning “green chemistry” have made the enzymes attractive industrial catalysts, as they can be used in mild reaction conditions [4,5,6]
We reported a free and immobilized LecitaseTM Ultra-catalyzed kinetic resolution of (E)-4-arylbut-3-en-2-yl esters via their enantioselective hydrolysis [33,34]
LecitaseTM Ultra (LU) was physically adsorbed on SupeliteTM DAX-8 polyacrylic resin (LU-DAX), covalently bound to cyanogen bromide-activated agarose (LU-CNBr), covalently bound to bacterial cellulose that was produced by Komagataeibacter xylinus and modified with polyethyleneimine, saturated by superparamagnetic Fe3 O4 particles, and activated by glutaraldehyde (LU-MBC)
Summary
Using enzymes as the biocatalysts of chemical reactions is a subject of interest for many researchers worldwide due to their wide spectrum of activity and high stereo- and regioselectivity [1,2,3].New environmental requirements concerning “green chemistry” have made the enzymes attractive industrial catalysts, as they can be used in mild reaction conditions (aqueous phase, normal pressure, room temperature) [4,5,6]. One of them is a production of chimeric enzymes by mixing the genes of two different proteins to join their desired properties [10,11,12] An example of such an approach is a preparation named LecitaseTM Ultra (LU), produced initially by Novo Nordisk A/S by the fusion of genes of the lipase from Thermomyces lanuginosus and phospholipase A1 from Fusarium oxysporum [13]. This enzyme was designed for the degumming of plant oils, which is the first step in the rafination of vegetable oils.
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