New Tailor-Made Alkyl-Aldehyde Bifunctional Supports for Lipase Immobilization
Robson Carlos Alnoch 1,2
, Ricardo Rodrigues de Melo 1,3, Jose M. Palomo 1, Emanuel Maltempi de Souza 2, Nadia Krieger 4 and Cesar Mateo 1,*
, Ricardo Rodrigues de Melo 1,3, Jose M. Palomo 1, Emanuel Maltempi de Souza 2, Nadia Krieger 4 and Cesar Mateo 1,*
1
Departamento de Biocatálisis, Instituto de Catálisis y Petroleoquímica (CSIC), Marie Curie 2. Cantoblanco, Campus UAM, 28049 Madrid, Spain
2
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Paraná, Cx. P. 19081 Centro Politécnico, 81531-980 Curitiba, Paraná, Brazil
3
Departamento de Ciência de Alimentos, Faculdade de Engenharia de Alimentos (FEA), Universidade Estadual de Campinas, 13083-862 Campinas, São Paulo, Brazil
4
Departamento de Química, Universidade Federal do Paraná, Cx. P. 19081 Centro Politécnico, 81531-980 Curitiba, Paraná, Brazil
*
Author to whom correspondence should be addressed.
Academic Editor: David D. Boehr
Catalysts 2016, 6(12), 191; https://doi.org/10.3390/catal6120191
Received: 28 October 2016 / Revised: 24 November 2016 / Accepted: 27 November 2016 / Published: 30 November 2016
(This article belongs to the Special Issue Asymmetric and Selective Biocatalysis)
Abstract
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. View Full-TextKeywords:
regioselective hydrolysis; biocatalysis; lipase; interfacial activation; covalent immobilization; tailor-made supports; enzyme stabilization
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Alnoch, R.C.; Rodrigues de Melo, R.; Palomo, J.M.; Maltempi de Souza, E.; Krieger, N.; Mateo, C. New Tailor-Made Alkyl-Aldehyde Bifunctional Supports for Lipase Immobilization. Catalysts 2016, 6, 191.
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