Lipase immobilization on smectite nanoclays:Characterization and application to the epoxidation of alpha-pinene

The immobilization of lipase B from Candida antarctica on smectite group nanoclays (Laponite, SWy-2 and Kunipia), as well as on their organically modified derivatives, was investigated. A combination of techniques, namely X-ray diffraction, thermal analysis, X-ray photoelectron and FT-IR spectroscop...

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Bibliographic Details
Published in:Bioresource Technology
Main Authors: Tzialla, Aikaterini A., Pavlidis, Ioannis V., Felicissimo, Marcella P., Rudolf, Petra, Gournis, Dimitrios, Stamatis, Haralambos
Format: Article in Journal/Newspaper
Language:English
Published: 2010
Subjects:
Lipase
Clays
Immobilization
Epoxidation
Structure
ORGANIC-SOLVENT
CHEMOENZYMATIC EPOXIDATION
CATALYZED SYNTHESIS
ENZYME-ACTIVITY
STABILITY
ENANTIOSELECTIVITY
NANOCOMPOSITES
CONFORMATION
ADSORPTION
SUPPORTS
Antarc*
Antarctica
Online Access:https://hdl.handle.net/11370/fdd91877-2f8e-479f-a940-9e29f74b49a1
https://research.rug.nl/en/publications/fdd91877-2f8e-479f-a940-9e29f74b49a1
https://doi.org/10.1016/j.biortech.2009.10.023
https://pure.rug.nl/ws/files/6741757/2010BioresourTechnolTzialla.pdf
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Summary:The immobilization of lipase B from Candida antarctica on smectite group nanoclays (Laponite, SWy-2 and Kunipia), as well as on their organically modified derivatives, was investigated. A combination of techniques, namely X-ray diffraction, thermal analysis, X-ray photoelectron and FT-IR spectroscopy, was used for characterization of the novel immobilized biocatalyst. Structural and biochemical characterization have revealed that the hydrophobic microenvironment created by the organo-modified clays induces minor changes on the secondary structure of the enzyme, resulting in enhanced catalytic behaviour in hydrophobic media. The immobilized lipase on such modified nanoclays can be effectively applied for the indirect epoxidation of alpha-pinene using hydrogen peroxide as substrate. The amount of alpha-pinene epoxide produced in a single-step biocatalytic process is up to 3-fold higher than that of free enzyme or enzyme immobilized in non-modified clays. Moreover, lipase immobilized in modified clays retains up to 90% of its initial activity, even after 48 h of incubation in the presence of oxidant, and up to 60% after four reaction cycles, while other forms of the enzyme retain less than 10%. (C) 2009 Elsevier Ltd. All rights reserved.

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