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

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 effi...

Full description

Bibliographic Details
Published in:Polymers
Main Authors: Hale Öztürk, Eric Pollet, Vincent Phalip, Yüksel Güvenilir, Luc Avérous
Format: Text
Language:English
Published: Multidisciplinary Digital Publishing Institute 2016
Subjects:
Online Access:https://doi.org/10.3390/polym8120416
_version_ 1821692625495785472
author Hale Öztürk
Eric Pollet
Vincent Phalip
Yüksel Güvenilir
Luc Avérous
author_facet Hale Öztürk
Eric Pollet
Vincent Phalip
Yüksel Güvenilir
Luc Avérous
author_sort Hale Öztürk
collection MDPI Open Access Publishing
container_issue 12
container_start_page 416
container_title Polymers
container_volume 8
description 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.
format Text
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
id ftmdpi:oai:mdpi.com:/2073-4360/8/12/416/
institution Open Polar
language English
op_collection_id ftmdpi
op_doi https://doi.org/10.3390/polym8120416
op_relation https://dx.doi.org/10.3390/polym8120416
op_rights https://creativecommons.org/licenses/by/4.0/
op_source Polymers; Volume 8; Issue 12; Pages: 416
publishDate 2016
publisher Multidisciplinary Digital Publishing Institute
record_format openpolar
spelling ftmdpi:oai:mdpi.com:/2073-4360/8/12/416/ 2025-01-16T19:15:15+00:00 Nanoclays for Lipase Immobilization: Biocatalyst Characterization and Activity in Polyester Synthesis Hale Öztürk Eric Pollet Vincent Phalip Yüksel Güvenilir Luc Avérous 2016-12-01 application/pdf https://doi.org/10.3390/polym8120416 EN eng Multidisciplinary Digital Publishing Institute https://dx.doi.org/10.3390/polym8120416 https://creativecommons.org/licenses/by/4.0/ Polymers; Volume 8; Issue 12; Pages: 416 Candida antarctica lipase B immobilization sepiolite montmorillonite organoclay ε-caprolactone polymerization Text 2016 ftmdpi https://doi.org/10.3390/polym8120416 2023-07-31T21:00:03Z 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. Text Antarc* Antarctica MDPI Open Access Publishing Polymers 8 12 416
spellingShingle Candida antarctica lipase B
immobilization
sepiolite
montmorillonite
organoclay
ε-caprolactone polymerization
Hale Öztürk
Eric Pollet
Vincent Phalip
Yüksel Güvenilir
Luc Avérous
Nanoclays for Lipase Immobilization: Biocatalyst Characterization and Activity in Polyester Synthesis
title Nanoclays for Lipase Immobilization: Biocatalyst Characterization and Activity in Polyester Synthesis
title_full Nanoclays for Lipase Immobilization: Biocatalyst Characterization and Activity in Polyester Synthesis
title_fullStr Nanoclays for Lipase Immobilization: Biocatalyst Characterization and Activity in Polyester Synthesis
title_full_unstemmed Nanoclays for Lipase Immobilization: Biocatalyst Characterization and Activity in Polyester Synthesis
title_short Nanoclays for Lipase Immobilization: Biocatalyst Characterization and Activity in Polyester Synthesis
title_sort nanoclays for lipase immobilization: biocatalyst characterization and activity in polyester synthesis
topic Candida antarctica lipase B
immobilization
sepiolite
montmorillonite
organoclay
ε-caprolactone polymerization
topic_facet Candida antarctica lipase B
immobilization
sepiolite
montmorillonite
organoclay
ε-caprolactone polymerization
url https://doi.org/10.3390/polym8120416