ReviewMicroorganisms2026
Review of Xylanases: Sources, Engineering and Biotechnological Use.
Review in Microorganisms, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed.
- Structure of recombinant Thermoascus aurantiacus xylanase TaXyn10 with an authentic N-terminal pyroglutamate.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Endo-β-1,4-Xylanase GH10 fromInternational journal of molecular sciences · 2026Article
- Production of Thermostable Xylanase byJournal of fungi (Basel, Switzerland) · 2026Article
- A thermostable GH10 xylanase from Anoxybacteroides tepidamans: structural insights and biochemical characterization.Molecular biology reports · 2026Article
- Advances in Enzymatic Production of Prebiotic Oligosaccharides from Agro-Industrial Waste: A Critical Review and Industrial Framework.Foods (Basel, Switzerland) · 2026Review
- Structural basis for inhibition of TcrXyn10A xylanase by nonspecific xylose binding at subsite - 2.Scientific reports · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors.
Funding
Abstract
Xylanases (EC 3.2.1.8) are value-added enzymes essential for biomass deconstruction and are widely used in the pulp and paper, food, feed, and biofuel sectors. This review provides a comprehensive analysis of the current state and future prospects of xylanase research and application. It begins by examining the structural diversity of xylan substrates and the corresponding classification of xylanase enzymes, their catalytic mechanisms, and methods for their functional study, such as inhibitor analysis. The discussion then covers the challenges and methods involved in the purification of xylanases from complex biological mixtures. While natural microbial sources (fungi and bacteria) remain important, the limitations of wild-type (WT) strains for industrial production are highlighted. The review assesses the most common recombinant production systems, including
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.