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

• Main Authors: Robson Carlos Alnoch, Ricardo Rodrigues de Melo, Jose M. Palomo, Emanuel Maltempi de Souza, Nadia Krieger, Cesar Mateo
• Format: Article
• Language: English
• Published: MDPI AG 2016-11-01
• Series: Catalysts
• Subjects: regioselective hydrolysis; biocatalysis; lipase; interfacial activation; covalent immobilization; tailor-made supports; enzyme stabilization
• Online Access: http://www.mdpi.com/2073-4344/6/12/191

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.