nanoclays for lipase immobilization: biocatalyst characterization and activity in polyester synthesis
Clicks: 226
ID: 185815
2016
Article Quality & Performance Metrics
Overall Quality
Improving Quality
0.0
/100
Combines engagement data with AI-assessed academic quality
Reader Engagement
Steady Performance
30.0
/100
221 views
15 readers
Trending
AI Quality Assessment
Not analyzed
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.
| Reference Key |
ztrk2016polymersnanoclays
Use this key to autocite in the manuscript while using
SciMatic Manuscript Manager or Thesis Manager
|
|---|---|
| Authors | ;Hale Öztürk;Eric Pollet;Vincent Phalip;Yüksel Güvenilir;Luc Avérous |
| Journal | Journal of Fluorescence |
| Year | 2016 |
| DOI |
10.3390/polym8120416
|
| URL | |
| Keywords |
Citations
No citations found. To add a citation, contact the admin at info@scimatic.org
Comments
No comments yet. Be the first to comment on this article.