Issue 21, 2022

Magnetic cross-linked enzyme aggregate based on ionic liquid modification as a novel immobilized biocatalyst for phytosterol esterification

Abstract

A lipase from Candida rugosa (CRL) is an efficient enzyme for phytosterol esterification. However, its poor stability limits its application. A novel cross-linked enzyme aggregate of CRL (CRL-FIL-CLEAs@Fe3O4) was designed by lipase surface modification with a functional ionic liquid (FIL) and immobilization with magnetic Fe3O4 nanoparticles as carriers simultaneously. The loading of CRL was 0.16 mg protein per mg CRL-FIL-CLEAs@Fe3O4. The hydrolysis expressed activity of CRL-FIL-CLEAs@Fe3O4 was 1.36 ± 0.04 U per mg CRL-FIL-CLEAs@Fe3O4. The hydrolysis specific activity of CRL-FIL-CLEAs@Fe3O4 (8.48 ± 0.25 U per mg protein) was significantly higher than that of conventional CRL-CLEAs (2.86 ± 0.26 U per mg protein). After 15 days of storage at room temperature, CRL-FIL-CLEAs@Fe3O4 exhibited 2.6 times higher activity (73.31%) than free lipases (28.52%). After eleven times of reuse, CRL-FIL-CLEAs@Fe3O4 still retained a high hydrolysis activity (83.42%). CRL-FIL-CLEAs@Fe3O4 was further applied in the solvent-free esterification reaction of phytosterol with oleic acid, and the conversion rate of phytosterol was up to 93.24% after 22 hours (the reaction temperature was 48 °C, the substrate molar ratio of oleic acids to phytosterols was 10 : 1, and the amount of biocatalysts and substrate phytosterol was 5 mg and 0.1 mmol, respectively). It was expected that a good reference could be provided for the more efficient and green production of food-grade phytosterol esters.

Graphical abstract: Magnetic cross-linked enzyme aggregate based on ionic liquid modification as a novel immobilized biocatalyst for phytosterol esterification

Supplementary files

Article information

Article type
Paper
Submitted
16 5月 2022
Accepted
09 9月 2022
First published
10 9月 2022

Catal. Sci. Technol., 2022,12, 6405-6415

Magnetic cross-linked enzyme aggregate based on ionic liquid modification as a novel immobilized biocatalyst for phytosterol esterification

Z. Bin, F. Ting, Y. Yan, L. Feng, O. Adesanya Idowu and S. Hongbo, Catal. Sci. Technol., 2022, 12, 6405 DOI: 10.1039/D2CY00882C

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

Spotlight

Advertisements