INBA   12521
INSTITUTO DE INVESTIGACIONES EN BIOCIENCIAS AGRICOLAS Y AMBIENTALES
Unidad Ejecutora - UE
artículos
Título:
Neotropical termite microbiomes as sources of novel plant cell wall degrading enzymes
Autor/es:
ROMERO VICTORICA, MATIAS; CEJA-NAVARRO, JAVIER A.; ONTAÑON, ORNELLA; QUINTERO GARCÍA, OMAR JASIEL; COWAN, DONALD; SORIA, MARCELO A.; VIKRAM, SURENDRA; GHIO, SILVINA; ETCHEVERRY, CLARA; ARNEODO, JOEL; BATISTA-GARCÍA, RAMÓN ALBERTO; ORTIZ, MAXIMILIANO; MARTÍNEZ-ÁVILA, LILIANA; CAMPOS, ELEONORA; TALIA, PAOLA M.
Revista:
Scientific Reports
Editorial:
Nature Publishing Group
Referencias:
Lugar: London; Año: 2020 vol. 10 p. 1 - 14
Resumen:
In this study, we used shotgun metagenomic sequencing to characterise the microbial metabolic potential for lignocellulose transformation in the gut of two colonies of Argentine higher termite species with diferent feeding habits, Cortaritermes fulviceps and Nasutitermes aquilinus. Our goal was to assess the microbial community compositions and metabolic capacity, and to identify genesinvolved in lignocellulose degradation. Individuals from both termite species contained the same fve dominant bacterial phyla (Spirochaetes, Firmicutes, Proteobacteria, Fibrobacteres and Bacteroidetes) although with diferent relative abundances. However, detected functional capacity varied, with C. fulviceps (a grass-wood-feeder) gut microbiome samples containing more genes related to amino acid metabolism, whereas N. aquilinus (a wood-feeder) gut microbiome samples were enriched in genes involved in carbohydrate metabolism and cellulose degradation. The C. fulviceps gut microbiome was enriched specifcally in genes coding for debranching- and oligosaccharide-degrading enzymes. These fndings suggest an association between the primary food source and the predicted categories of the enzymes present in the gut microbiomes of each species. To further investigate the termite microbiomes as sources of biotechnologically relevant glycosyl hydrolases, a putative GH10 endo-β-1,4- xylanase, Xyl10E, was cloned and expressed in Escherichia coli. Functional analysis of the recombinantmetagenome-derived enzyme showed high specifcity towards beechwood xylan (288.1 IU/mg), with the optimum activity at 50 °C and a pH-activity range from 5 to 10. These characteristics suggest that Xy110E may be a promising candidate for further development in lignocellulose deconstruction applications.