Issue 12, 2021

Lipase on carbon nanotubes – an active, selective, stable and easy-to-optimize nanobiocatalyst for kinetic resolutions

Abstract

An efficient nanobioconjugate of lipase B from Candida antarctica was prepared by covalent binding onto carboxy-functionalized single-walled carbon nanotubes and tested in batch and flow modes for the enzymatic kinetic resolution of several racemic secondary 1-arylethan-1-ols. The influence of various process parameters such as temperature, flow rate and substrate concentration upon the biocatalyst efficiency and selectivity in the kinetic resolution of rac-1-phenylethan-1-ol was investigated and the conditions for the highest productivity were determined. The long-term activity and selectivity of the biocatalyst were preserved, enabling hundred gram scale resolution of rac-1-phenylethan-1-ol with only ∼70 mg of biocatalyst.

Graphical abstract: Lipase on carbon nanotubes – an active, selective, stable and easy-to-optimize nanobiocatalyst for kinetic resolutions

Supplementary files

Article information

Article type
Paper
Submitted
16 Aug 2021
Accepted
21 Sep 2021
First published
21 Sep 2021

React. Chem. Eng., 2021,6, 2391-2399

Lipase on carbon nanotubes – an active, selective, stable and easy-to-optimize nanobiocatalyst for kinetic resolutions

C. A. Gal, L. E. Barabás, J. Bartha Vári, M. E. Moisă, D. Balogh-Weiser, L. C. Bencze, L. Poppe, C. Paizs and M. I. Toșa, React. Chem. Eng., 2021, 6, 2391 DOI: 10.1039/D1RE00342A

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