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New Tailor-Made Alkyl-Aldehyde Bifunctional Supports for Lipase Immobilization

AutorAlnoch, Robson Carlos; Rodrigues de Melo, Ricardo; Palomo, José Miguel ; Maltempi de Souza, Emanuel; Krieger, Nadia; Mateo, César
Fecha de publicación30-nov-2016
EditorMultidisciplinary Digital Publishing Institute
CitaciónCatalysts 6(12): 191 (2016)
ResumenImmobilized and stabilized lipases are important biocatalytic tools. In this paper, different tailor-made bifunctional supports were prepared for the immobilization of a new metagenomic lipase (LipC12). The new supports contained hydrophobic groups (different alkyl groups) to promote interfacial adsorption of the lipase and aldehyde groups to react covalently with the amino groups of side chains of the adsorbed lipase. The best catalyst was 3.5-fold more active and 5000-fold more stable than the soluble enzyme. It was successfully used in the regioselective deacetylation of peracetylated <span style="font-variant: small-caps;">d</span>-glucal. The PEGylated immobilized lipase showed high regioselectivity, producing high yields of the C-3 monodeacetylated product at pH 5.0 and 4 °C.
URIhttp://hdl.handle.net/10261/142161
DOIhttp://dx.doi.org/doi: 10.3390/catal6120191
Identificadoresdoi: 10.3390/catal6120191
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