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Cross-linking of a polyketide synthase domain leads to a recyclable biocatalyst for chiral oxygen heterocycle synthesis

Title data

Wagner, Lisa Maria Carolin ; Roß, Theresa ; Hollmann, Tim ; Hahn, Frank:
Cross-linking of a polyketide synthase domain leads to a recyclable biocatalyst for chiral oxygen heterocycle synthesis.
In: RSC Advances. Vol. 11 (2021) Issue 33 . - pp. 20248-20251.
ISSN 2046-2069
DOI: https://doi.org/10.1039/D1RA03692K

Project information

Project financing: Deutsche Forschungsgemeinschaft
DFG-Sachbeihilfe
Promotionsstipendium der Deutschen Bundesstiftung Umwelt

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professor Organic Chemistry - Food Chemistry > Professor Organic Chemistry - Food Chemistry - Univ.-Prof. Dr. Frank Hahn
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 27 Jul 2021 06:47
Last Modified: 27 Jul 2021 06:47
URI: https://eref.uni-bayreuth.de/id/eprint/66696