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

Immobilized 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 ads...

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Published inCatalysts Vol. 6; no. 12; p. 191
Main Authors Alnoch, Robson, Rodrigues de Melo, Ricardo, Palomo, Jose, Maltempi de Souza, Emanuel, Krieger, Nadia, Mateo, Cesar
Format Journal Article
LanguageEnglish
Published Basel MDPI AG 01.12.2016
Subjects
Adsorption
biocatalysis
Catalysis
Catalysts
Chemical reactions
Covalence
covalent immobilization
enzyme stabilization
Enzymes
Immobilization
interfacial activation
Lipase
regioselective hydrolysis
tailor-made supports
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Summary:Immobilized 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 d-glucal. The PEGylated immobilized lipase showed high regioselectivity, producing high yields of the C-3 monodeacetylated product at pH 5.0 and 4 °C.
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ISSN:2073-4344
2073-4344
DOI:10.3390/catal6120191