Unraveling the xylanolytic potential of Acidobacteria bacterium AB60 from Cerrado soils
Autor: | Gabriel Fernandes, Gisele Regina Rodrigues, Eiko E. Kuramae, Luís Felipe Schroeder, Otávio Henrique Bezerra Pinto, Cristine Chaves Barreto, Betania Ferraz Quirino, Ohana Y. A. Costa |
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Přispěvatelé: | Microbial Ecology (ME) |
Jazyk: | angličtina |
Rok vydání: | 2020 |
Předmět: |
animal structures
Cellulase Microbiology Cell wall 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Polysaccharides RNA Ribosomal 16S Genetics medicine α-l-rhamnosidase Glycoside hydrolase Hemicellulose Cellulose Molecular Biology Phylogeny Soil Microbiology 030304 developmental biology 0303 health sciences biology 030306 microbiology Chemistry Hydrolysis food and beverages Cerrado Plan_S-Compliant_NO cellulases biology.organism_classification Xylan Carboxymethyl cellulose Acidobacteria carbohydrates (lipids) Biochemistry international biology.protein xylanases Pectins Xylans functional genomics Brazil Genome Bacterial medicine.drug |
Zdroj: | FEMS Microbiology Letters, 367(18):fnaa149. Wiley-Blackwell |
ISSN: | 0378-1097 |
Popis: | The presence of genes for glycosyl hydrolases in many Acidobacteria genomes indicates an important role in the degradation of plant cell wall material. Acidobacteria bacterium AB60 was obtained from Cerrado oligotrophic soil in Brazil, where this phylum is abundant. The 16S rRNA gene analyses showed that AB60 was closely related to the genera Occallatibacter and Telmatobacter. However, AB60 grew on xylan as carbon source, which was not observed in Occallatibacter species; but growth was not detected on medium containing carboxymethyl cellulose, as observed in Telmatobacter. Nevertheless, the genome analysis of AB60 revealed genes for the enzymes involved in cellulose as well as xylan degradation. In addition to enzymes involved in xylan degradation, α-l-rhamnosidase was detected in the cultures of AB60. Functional screening of a small-insert genomic library did not identify any clones capable of carboxymethyl cellulose degradation, but open reading frames coding α-l-arabinofuranosidase and α-l-rhamnosidase were present in clones showing xylan degradation halos. Both enzymes act on the lateral chains of heteropolymers such as pectin and some hemicelluloses. These results indicate that the hydrolysis of α-linked sugars may offer a metabolic niche for slow-growing Acidobacteria, allowing them to co-exist with other plant-degrading microbes that hydrolyze β-linked sugars from cellulose or hemicellulose backbones. |
Databáze: | OpenAIRE |
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