A robust and efficient lipase based nanobiocatalyst for phenothiazinyl-ethanol resolution

Abstract

A new robust, active and selective biocatalyst, prepared by CaL-B entrapment into polyvinyl alcohol–chitosan nanofibers, proved to be efficient for the EKR of nine racemic phenothiazinyl-ethanols, important chiral building blocks.

Abstract

A new robust, active and selective biocatalyst was prepared by entrapment of lipase B from Candida antarctica into polyvinyl alcohol–chitosan nanofibers. The influence of the most important process parameters on biocatalyst activity and selectivity was studied and the substrate domain was finally investigated. The developed biocatalyst presents high activity and selectivity and excellent stability for synthetic application, preserving more that 95% activity even after 10 reaction cycles, and is efficient for the enzymatic kinetic resolution of nine racemic phenothiazinyl-ethanols, especially for N-ethyl and N-butyl derivatives, bulky substrates with high relevance as chiral building blocks.