ReviewEssays in biochemistry2023
Glucuronoyl esterases - enzymes to decouple lignin and carbohydrates and enable better utilization of renewable plant biomass.
Review in Essays in biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Microbial community characterization in semi-hydroponic systems of Starbor kale (Current research in microbial sciences · 2026Article
- Utilisation of mango seed husk for the production of phenolic compounds and glucose with C1184 enzyme preparation reveals the role of glucuronoyl esters in lignin-carbohydrate linkages in biomass recalcitrance.Bioresources and bioprocessing · 2025Article
- Insights into a water-mediated catalytic triad architecture in CE20 carbohydrate esterases.Nature communications · 2025Article
- Biochemical Characterization of Multimodular Xylanolytic Carbohydrate Esterases from the Marine Bacterium Flavimarina sp. Hel_I_48.Chembiochem : a European journal of chemical biology · 2025Article
- Fungal Coculture: Unlocking the Potential for Efficient Bioconversion of Lignocellulosic Biomass.Journal of fungi (Basel, Switzerland) · 2025Review
- Structural, Biochemical, and Phylogenetic Analysis of Bacterial and Fungal Carbohydrate Esterase Family 15 Glucuronoyl Esterases in the Rumen.The protein journal · 2024Article
- Modifying lignin composition and xylan O-acetylation induces changes in cell wall composition, extractability, and digestibility.Biotechnology for biofuels and bioproducts · 2024Article
- Exploration of three Dyadobacter fermentans enzymes uncovers molecular activity determinants in CE15.Applied microbiology and biotechnology · 2024Article
- Transesterification with CE15 glucuronoyl esterase from Cerrena unicolor reveals substrate preferences.Biotechnology letters · 2024Article
- Polysaccharide utilization loci from Bacteroidota encode CE15 enzymes with possible roles in cleaving pectin-lignin bonds.Applied and environmental microbiology · 2024Article
- New insights to diversity and enzyme-substrate interactions of fungal glucuronoyl esterases.Applied microbiology and biotechnology · 2023Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glucuronoyl esterases (GEs) are microbial enzymes able to cleave covalent linkages between lignin and carbohydrates in the plant cell wall. GEs are serine hydrolases found in carbohydrate esterase family 15 (CE15), which belongs to the large α/β hydrolase superfamily. GEs have been shown to reduce plant cell wall recalcitrance by hydrolysing the ester bonds found between glucuronic acid moieties on xylan polysaccharides and lignin. In recent years, the exploration of CE15 has broadened significantly and focused more on bacterial enzymes, which are more diverse in terms of sequence and structure to their fungal counterparts. Similar to fungal GEs, the bacterial enzymes are able to improve overall biomass deconstruction but also appear to have less strict substrate preferences for the uronic acid moiety. The structures of bacterial GEs reveal that they often have large inserts close to the active site, with implications for more extensive substrate interactions than the fungal GEs which have more open active sites. In this review, we highlight the recent work on GEs which has predominantly regarded bacterial enzymes, and discuss similarities and differences between bacterial and fungal enzymes in terms of the biochemical properties, diversity in sequence and modularity, and structural variations that have been discovered thus far in CE15.
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