Jump to main content
Jump to site search
SCHEDULED MAINTENANCE Close the message box

Maintenance work is planned for Monday 16 August 2021 from 07:00 to 23:59 (BST).

Website performance may be temporarily affected and you may not be able to access some PDFs or images. If this does happen, refreshing your web browser should resolve the issue. We apologise for any inconvenience this might cause and thank you for your patience.


Issue 19, 2018

Rationally designing hydrophobic UiO-66 support for the enhanced enzymatic performance of immobilized lipase

Author affiliations

Abstract

The immobilization of Aspergillus niger lipase (ANL) on UiO-66 (a typical MOF), the effect of support hydrophobicity on lipase's immobilization as well as the enzymatic performance for biodiesel preparation was explored in this enzyme/MOF system. First, the hydrophobic UiO-66 was obtained by polydimethylsiloxane (PDMS) coating, and then used as the immobilization carrier for physically adsorbing ANL through hydrophobic interactions. It was found that the properties of immobilized ANL were remarkably enhanced through hydrophobic modification of UiO-66. ANL immobilized on hydrophobic UiO-66 presented much higher enzymatic activity and activity recovery compared with those of ANL on pristine UiO-66. In the catalysis of lipase-mediated biodiesel production, ANL immobilized on hydrophobic UiO-66-PDMS-6 h performed at a faster reaction rate and gave a much higher yield than its counterpart. A biodiesel yield of 88% was afforded by ANL/UiO-66-PDMS-6 h at 24 h, and the immobilized lipase demonstrated a rather good reusability, with 83.0% activity remaining after ten successive operations.

Graphical abstract: Rationally designing hydrophobic UiO-66 support for the enhanced enzymatic performance of immobilized lipase

Article information


Submitted
24 Apr 2018
Accepted
29 Aug 2018
First published
30 Aug 2018

Green Chem., 2018,20, 4500-4506
Article type
Paper

Rationally designing hydrophobic UiO-66 support for the enhanced enzymatic performance of immobilized lipase

Y. Hu, L. Dai, D. Liu and W. Du, Green Chem., 2018, 20, 4500 DOI: 10.1039/C8GC01284A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.


Social activity

Search articles by author

Spotlight

Advertisements