ArticleBMC biotechnology2013
Identification of an endo-1,4-beta-xylanase of Ustilago maydis.
Article in BMC biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 45 citations in OpenAlex.
- Sampling-free investigation of microbial carbon source preferences on renewable feedstocks via online monitoring of oxygen transfer rate.Bioprocess and biosystems engineering · 2025Article
- Monitoring corn stover processing by the fungus Ustilago maydis.Bioresources and bioprocessing · 2024Article
- Establishing an itaconic acid production process with Ustilago species on the low-cost substrate starch.FEMS yeast research · 2024Article
- Article
- High level production of itaconic acid at low pH by Ustilago maydis with fed-batch fermentation.Bioprocess and biosystems engineering · 2021Article
- Bioprospecting of microbial strains for biofuel production: metabolic engineering, applications, and challenges.Biotechnology for biofuels · 2021Review
- Consolidated bioprocessing of cellulose to itaconic acid by a co-culture of Trichoderma reesei and Ustilago maydis.Biotechnology for biofuels · 2020Article
- An Ustilago maydis chassis for itaconic acid production without by-products.Microbial biotechnology · 2020Article
- New Insights of Ustilago maydis as Yeast Model for Genetic and Biotechnological Research: A Review.Current microbiology · 2019Review
- From beech wood to itaconic acid: case study on biorefinery process integration.Biotechnology for biofuels · 2018Review
- Metabolic engineering ofMetabolic engineering communications · 2017Article
- Efficient itaconic acid production from glycerol withBiotechnology for biofuels · 2017Article
- Promoters from the itaconate cluster ofFungal biology and biotechnology · 2017Article
- Activating Intrinsic Carbohydrate-Active Enzymes of the Smut Fungus Ustilago maydis for the Degradation of Plant Cell Wall Components.Applied and environmental microbiology · 2016Article
- Phylogenetic analysis of β-xylanase SRXL1 of Sporisorium reilianum and its relationship with families (GH10 and GH11) of Ascomycetes and Basidiomycetes.Scientific reports · 2016Article
- Prospecting the biodiversity of the fungal family Ustilaginaceae for the production of value-added chemicals.Fungal biology and biotechnology · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe utilization of raw biomass components such as cellulose or hemicellulose for the production of valuable chemicals has attracted considerable research interest in recent years. One promising approach is the application of microorganisms that naturally convert biomass constituents into value added chemicals. One of these organisms--Ustilago maydis--can grow on xylan, the second most abundant polysaccharide in nature, while at the same time it produces chemicals of biotechnological interest.
resultsIn this study, we present the identification of an endo-1,4-beta xylanase responsible for xylan degradation. Xylanase activity of U. maydis cells was indirectly detected by the quantification of released reducing sugars and could be confirmed by visualizing oligosaccharides as degradation products of xylan by thin layer chromatography. A putative endo-1,4-beta-xylanase, encoded by um06350.1, was identified in the supernatant of xylan-grown cells. To confirm the activity, we displayed the putative xylanase on the surface of the xylanase negative Saccharomyces cerevisiae EBY100. The presented enzyme converted xylan to xylotriose, similar to the source organism U. maydis.
conclusionsThe xylan degradation ability together with its unicellular and yeast-like growth makes U. maydis MB215 a promising candidate for the production of valuable chemicals such as itaconic acid or glycolipids from lignocellulosic biomass. Therefore, the characterization of the endo-1,4-beta-xylanase, encoded by um06350.1, is a further step towards the biotechnological application of U. maydis and its enzymes.
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