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Polymers 2016, 8(12), 416; doi:10.3390/polym8120416

Nanoclays for Lipase Immobilization: Biocatalyst Characterization and Activity in Polyester Synthesis

1
BioTeam/ICPEES-ECPM, UMR 7515, Université de Strasbourg, 25 rue Becquerel, 67087 Strasbourg, Cedex 2, France
2
Department of Chemical Engineering, Istanbul Technical University, Maslak, 34469 Istanbul, Turkey
*
Authors to whom correspondence should be addressed.
Academic Editor: Katja Loos
Received: 13 July 2016 / Revised: 24 November 2016 / Accepted: 28 November 2016 / Published: 1 December 2016
(This article belongs to the Special Issue Enzymatic Polymer Synthesis)
View Full-Text   |   Download PDF [2838 KB, uploaded 1 December 2016]   |  

Abstract

The immobilization of Candida antarctica lipase B (CALB) was performed by physical adsorption on both neat and organo-modified forms of sepiolite and montmorillonite. The influence of different parameters, e.g., solvent, enzyme loading, cross-linking, and type of clay support, on immobilization efficiency and catalyst hydrolytic activity has been investigated. The highest hydrolytic activities were obtained for CALB immobilized on organo-modified clay minerals, highlighting the beneficial effect of organo-modification. The esterification activity of these CALB/organoclay catalysts was also tested in the ring-opening polymerization of ε-caprolactone. The polymerization kinetics observed for clay-immobilized catalysts confirmed that CALB adsorbed on organo-modified montmorillonite (CALB/MMTMOD) was the highest-performing catalytic system. View Full-Text
Keywords: Candida antarctica lipase B; immobilization; sepiolite; montmorillonite; organoclay; ε-caprolactone polymerization Candida antarctica lipase B; immobilization; sepiolite; montmorillonite; organoclay; ε-caprolactone polymerization
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MDPI and ACS Style

Öztürk, H.; Pollet, E.; Phalip, V.; Güvenilir, Y.; Avérous, L. Nanoclays for Lipase Immobilization: Biocatalyst Characterization and Activity in Polyester Synthesis. Polymers 2016, 8, 416.

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