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, Advance Article

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, Advance Article , DOI: 10.1039/D1RE00342A

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