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Int. J. Mol. Sci. 2018, 19(2), 553; doi:10.3390/ijms19020553

Stabilization of Immobilized Lipases by Intense Intramolecular Cross-Linking of Their Surfaces by Using Aldehyde-Dextran Polymers

1
Department of Biocatalysis, Institute of Catalysis and Petrochemistry, Consejo Superior de Investigaciones Científicas (CSIC), 28049 Madrid, Spain
2
Department of Chemistry, Kharazmi University, 1417466191 Tehran, Iran
3
Pharmacy and Biotechnology Department, School of Biomedical Sciences, Universidad Europea de Madrid, Villaviciosa de Odón, 28670 Madrid, Spain
4
Departamento de Química, Universidad de Guadalajara, Guadalajara 44430, Jalisco, Mexico
*
Authors to whom correspondence should be addressed.
Received: 22 January 2018 / Revised: 6 February 2018 / Accepted: 7 February 2018 / Published: 12 February 2018
(This article belongs to the Special Issue Immobilization of Microorganisms and Enzymes)
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Abstract

Immobilized enzymes have a very large region that is not in contact with the support surface and this region could be the target of new stabilization strategies. The chemical amination of these regions plus further cross-linking with aldehyde-dextran polymers is proposed here as a strategy to increase the stability of immobilized enzymes. Aldehyde-dextran is not able to react with single amino groups but it reacts very rapidly with polyaminated surfaces. Three lipases—from Thermomyces lanuginosus (TLL), Rhizomucor miehiei (RML), and Candida antarctica B (CALB)—were immobilized using interfacial adsorption on the hydrophobic octyl-Sepharose support, chemically aminated, and cross-linked. Catalytic activities remained higher than 70% with regard to unmodified conjugates. The increase in the amination degree of the lipases together with the increase in the density of aldehyde groups in the dextran-aldehyde polymer promoted a higher number of cross-links. The sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis of those conjugates demonstrates the major role of the intramolecular cross-linking on the stabilization of the enzymes. The highest stabilization was achieved by the modified RML immobilized on octyl-Sepharose, which was 250-fold more stable than the unmodified conjugate. The TLL and the CALB were 40-fold and 4-fold more stable than the unmodified conjugate. View Full-Text
Keywords: enzyme stabilization; lipase immobilization; stabilizing polymers; chemical amination; enzyme cross-linking; aldehyde–dextran enzyme stabilization; lipase immobilization; stabilizing polymers; chemical amination; enzyme cross-linking; aldehyde–dextran
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MDPI and ACS Style

Orrego, A.H.; Ghobadi, R.; Moreno-Perez, S.; Mendoza, A.J.; Fernandez-Lorente, G.; Guisan, J.M.; Rocha-Martin, J. Stabilization of Immobilized Lipases by Intense Intramolecular Cross-Linking of Their Surfaces by Using Aldehyde-Dextran Polymers. Int. J. Mol. Sci. 2018, 19, 553.

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