Identification of an endo-1,4-beta-xylanase of Ustilago maydis. 2013

Elena Geiser, and Nick Wierckx, and Martin Zimmermann, and Lars M Blank
iAMB-Institute of Applied Microbiology, ABBt-Aachen Biology and Biotechnology, RWTH Aachen University, Worringerweg 1, Aachen D-52074, Germany.

BACKGROUND The 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. RESULTS In 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. CONCLUSIONS The 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.

UI MeSH Term Description Entries
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D005656 Fungal Proteins Proteins found in any species of fungus. Fungal Gene Products,Fungal Gene Proteins,Fungal Peptides,Gene Products, Fungal,Yeast Proteins,Gene Proteins, Fungal,Peptides, Fungal,Proteins, Fungal
D006863 Hydrogen-Ion Concentration The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D012441 Saccharomyces cerevisiae A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement. Baker's Yeast,Brewer's Yeast,Candida robusta,S. cerevisiae,Saccharomyces capensis,Saccharomyces italicus,Saccharomyces oviformis,Saccharomyces uvarum var. melibiosus,Yeast, Baker's,Yeast, Brewer's,Baker Yeast,S cerevisiae,Baker's Yeasts,Yeast, Baker
D014312 Trisaccharides Oligosaccharides containing three monosaccharide units linked by glycosidic bonds. Trisaccharide
D014588 Ustilago A genus of basidiomycetous smut fungi comprising the loose smuts. Ustilagos
D014990 Xylans Polysaccharides consisting of xylose units. Xylan
D017353 Gene Deletion A genetic rearrangement through loss of segments of DNA or RNA, bringing sequences which are normally separated into close proximity. This deletion may be detected using cytogenetic techniques and can also be inferred from the phenotype, indicating a deletion at one specific locus. Deletion, Gene,Deletions, Gene,Gene Deletions
D043364 Endo-1,4-beta Xylanases Enzymes which catalyze the endohydrolysis of 1,4-beta-D-xylosidic linkages in XYLANS. Endo-1,4-beta-Xylanase,1,4-beta-D-Xylanohydrolase,Beta-1-4-Endoxylanase,Endo-1,4-Xylanase II,Endo-1,4-beta-Xylanase II,Endoxylanase,Xylanase A,Xylanase B,Xylanase C,Xylanase D,Xylanase J,Xylanase Y,Xylanase Z,beta Xylanase,1,4 beta D Xylanohydrolase,Beta 1 4 Endoxylanase,Endo 1,4 Xylanase II,Endo 1,4 beta Xylanase,Endo 1,4 beta Xylanase II,Endo 1,4 beta Xylanases,Xylanase, beta,Xylanases, Endo-1,4-beta
D061505 Cell Surface Display Techniques Techniques utilizing cells that express RECOMBINANT FUSION PROTEINS engineered to translocate through the CELL MEMBRANE and remain attached to the outside of the cell. Cell Surface Display Technology,Phage Display Techniques,Display Technique, Phage,Display Techniques, Phage,Phage Display Technique,Technique, Phage Display,Techniques, Phage Display

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