The structural basis of fungal glucuronoyl esterase activity on natural substrates

Heidi A. Ernst; Caroline Mosbech; Annette E. Langkilde; Peter Westh; Anne S. Meyer; Jane W. Agger; Sine Larsen

doi:10.1038/s41467-020-14833-9

Nature Communications (Feb 2020)

The structural basis of fungal glucuronoyl esterase activity on natural substrates

Heidi A. Ernst,
Caroline Mosbech,
Annette E. Langkilde,
Peter Westh,
Anne S. Meyer,
Jane W. Agger,
Sine Larsen

Affiliations

Heidi A. Ernst: Department of Chemistry, University of Copenhagen, Universitetsparken 5
Caroline Mosbech: Department of Biotechnology and Biomedicine, Technical University of Denmark
Annette E. Langkilde: Department of Drug Design and Pharmacology, University of Copenhagen, Universitetsparken 2
Peter Westh: Department of Biotechnology and Biomedicine, Technical University of Denmark
Anne S. Meyer: Department of Biotechnology and Biomedicine, Technical University of Denmark
Jane W. Agger: Department of Biotechnology and Biomedicine, Technical University of Denmark
Sine Larsen: Department of Chemistry, University of Copenhagen, Universitetsparken 5

DOI: https://doi.org/10.1038/s41467-020-14833-9
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 12

Abstract

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Glucuronoyl esterases have the potential to be used in the biocatalytic conversion of lignin-carbohydrate complexes to obtain pure lignin for downstream biofuel conversion. Here the authors present a detailed structural analysis of the glucuronoyl esterase from Cerrena unicolor, providing the basis for its activity on natural substrate and for how lignin can be selectively separated from lignocellulosic materials.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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