Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/357630
Type: Artigo
Title: New tailor-made alkyl-aldehyde bifunctional supports for lipase immobilization
Author: Alnoch, Robson Carlos
Melo, Ricardo Rodrigues de
Palomo, Jose M.
Souza, Emanuel Maltempi de
Krieger, Nadia
Mateo, Cesar
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.
Subject: Hidrólise
Biocatálise
Lipase
Country: Suíça
Editor: MDPI
Rights: Aberto
Identifier DOI: 10.3390/catal6120191
Address: https://www.mdpi.com/2073-4344/6/12/191
Date Issue: 2016
Appears in Collections:FEA - Artigos e Outros Documentos

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