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Molecules 2017, 22(1), 91; doi:10.3390/molecules22010091

Desorption of Lipases Immobilized on Octyl-Agarose Beads and Coated with Ionic Polymers after Thermal Inactivation. Stronger Adsorption of Polymers/Unfolded Protein Composites

1
CONACYT—Centro de Investigación en Alimentación y Desarrollo, A.C. (CIAD)—Centro de Innovación y Desarrollo Agroalimentario de Michoacán, A.C. (CIDAM), Km. 8 Antigua Carretera a Pátzcuaro s/n, C.P. 58341 Morelia, Michoacán, Mexico
2
Departamento de Biocatálisis, Instituto de Catálisis-CSIC, C/Marie Curie 2, Campus UAM-CSIC, Cantoblanco, 28049 Madrid, Spain
Both authors have evenly contributed to this paper.
*
Author to whom correspondence should be addressed.
Academic Editor: Derek J. McPhee
Received: 24 November 2016 / Revised: 2 January 2017 / Accepted: 3 January 2017 / Published: 5 January 2017
(This article belongs to the Special Issue Enzyme Immobilization 2016)
View Full-Text   |   Download PDF [1388 KB, uploaded 5 January 2017]   |  

Abstract

Lipases from Candida antarctica (isoform B) and Rhizomucor miehei (CALB and RML) have been immobilized on octyl-agarose (OC) and further coated with polyethylenimine (PEI) and dextran sulfate (DS). The enzymes just immobilized on OC supports could be easily released from the support using 2% SDS at pH 7, both intact or after thermal inactivation (in fact, after inactivation most enzyme molecules were already desorbed). The coating with PEI and DS greatly reduced the enzyme release during thermal inactivation and improved enzyme stability. However, using OC-CALB/RML-PEI-DS, the full release of the immobilized enzyme to reuse the support required more drastic conditions: a pH value of 3, a buffer concentration over 2 M, and temperatures above 45 °C. However, even these conditions were not able to fully release the thermally inactivated enzyme molecules from the support, being necessary to increase the buffer concentration to 4 M sodium phosphate and decrease the pH to 2.5. The formation of unfolded protein/polymers composites seems to be responsible for this strong interaction between the octyl and some anionic groups of OC supports. The support could be reused five cycles using these conditions with similar loading capacity of the support and stability of the immobilized enzyme. View Full-Text
Keywords: enzyme physical crosslinking with polymers; octyl-agarose; lipase immobilization; enzyme desorption; support reuse; enzyme inactivation enzyme physical crosslinking with polymers; octyl-agarose; lipase immobilization; enzyme desorption; support reuse; enzyme inactivation
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MDPI and ACS Style

Virgen-Ortíz, J.J.; Pedrero, S.G.; Fernandez-Lopez, L.; Lopez-Carrobles, N.; Gorines, B.C.; Otero, C.; Fernandez-Lafuente, R. Desorption of Lipases Immobilized on Octyl-Agarose Beads and Coated with Ionic Polymers after Thermal Inactivation. Stronger Adsorption of Polymers/Unfolded Protein Composites. Molecules 2017, 22, 91.

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