ArticleJournal of applied glycoscience2022
Acetylated Xylan Degradation by Glycoside Hydrolase Family 10 and 11 Xylanases from the White-rot Fungus
Article in Journal of applied glycoscience, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 17 citations in OpenAlex.
- Article
- Identification and structural characterization of a novel acetyl xylan esterase from Aspergillus oryzae.The FEBS journal · 2025Article
- Exploring the synergy between fungal CE15 glucuronoyl esterases and xylanases for lignocellulose saccharification.Biotechnology for biofuels and bioproducts · 2025Article
- Modification of xylan in secondary walls alters cell wall biosynthesis and wood formation programs and improves saccharification.Plant biotechnology journal · 2025Article
- Integrity of xylan backbone affects plant responses to drought.Frontiers in plant science · 2024Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Endo-type xylanases are key enzymes in microbial xylanolytic systems, and xylanases belonging to glycoside hydrolase (GH) families 10 or 11 are the major enzymes degrading xylan in nature. These enzymes have typically been characterized using xylan prepared by alkaline extraction, which removes acetyl sidechains from the substrate, and thus the effect of acetyl groups on xylan degradation remains unclear. Here, we compare the ability of GH10 and 11 xylanases,
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