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Updated: Sep 25, 2025

Enzymatic Cascade Reactions for the Synthesis of Chiral Amino Alcohols from L-lysine
Published on: February 16, 2018
Cross-linking of a polyketide synthase domain leads to a recyclable biocatalyst for chiral oxygen heterocycle
Lisa Wagner1, Theresa Roß1, Tim Hollmann1
1Department of Chemistry, Faculty of Biology, Chemistry and Earth Sciences, University of Bayreuth Universitätsstraße 30 95447 Bayreuth Germany frank.hahn@uni-bayreuth.de.
Abstract:
The potential of polyketide synthase (PKS) domains for chemoenzymatic synthesis can often not be tapped due to their low stability and activity in vitro. In this proof-of-principle study, the immobilisation of the heterocycle-forming PKS domain AmbDH3 as a cross-linked enzyme aggregate (CLEA) is described. The AmbDH3-CLEA showed good activity recovery, stability and recyclability. Repetitive reactions on the semi-preparative scale were performed with high conversion and isolated yield. Similar to that observed for the free enzyme, the aggregate retained substrate tolerance and the ability for kinetic resolution. This first example of a successful enzymatic PKS domain immobilisation demonstrates that cross-linking can in principle be applied to this type of enzyme to increase its applicability for chemoenzymatic synthesis.
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