Proteomic analysis of secretomes from Bacillus sp. AR03: characterization of enzymatic cocktails active on complex carbohydrates for xylooligosaccharides production

Bacillus sp. AR03 have been described as an important producer of carbohydrate-active enzymes (CAZymes) when growing in a peptone-based medium supplemented with simple sugars and/or carboxymethyl cellulose (CMC) as carbon sources. This work aimed to identify the extracellular enzymatic cocktails through shotgun proteomics. The proteomic analysis showed that enzymes involved in cellulose and xylan degradation were among the most abundant proteins. These enzymes included an endo-glucanase GH5_2 and a glucuronoxylanase GH30_8, which were found in all conditions. In addition, several proteins were differentially expressed in the three evaluated culture media, indicating microbial metabolic changes due to the different supplied carbon sources, particularly, in the presence of CMC. Finally, the capability of the crude enzymatic cocktails from culture media to degrade birchwood xylan was assessed, which produced mostly xylooligosaccharides containing among 3–5 xylose units. Consequently, this work shows the potential of the extracellular enzymes from Bacillus sp. AR03 for producing emergent prebiotics.Fil: Hero, Johan Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Pisa, José Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Raimondo, Enzo Emanuel. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Martínez, María Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentin

Synergistic effect of xylanases produced in co-culture of bacillus sp. Ar03 and paenibacillus sp. Ar247

In nature, the plant biomass is degraded by a process that requires the cooperative action of multiple microorganisms capable of producing a variety of enzymes to attack the complex structure of lignocelluloses. This work assessed the production and the enzymatic activity over the main hemicellulolytic fraction of plant biomass, xylan, in monoculture and co-culture systems of bacteria isolated from regional niches associated with sugar cane bagasse. The enzyme activity was estimated by measuring reducing sugars released using the dinitrosalicylic acid method. All cultivation assays were performed at 200 rpm and 30 °C in a diluted peptone broth supplemented with 1% CMC (w/v). The viability and the growth of both isolates were estimated by the number of colony forming units, fact that was possible since both isolates exhibited different colony morphology. The specific xylanolytic activity of the co-culture of Bacillus sp. AR03 and Paenibacillus sp. AR247 was of 7.03 ± 0.46 IU/mg and 8.36 ± 0.49 IU/mg at 48 h and 96 h of cultivation, respectively. In contrast, each isolate assayed simultaneously under identical conditions, produced significantly lower xylanase activities, even when both isolates grew similarly in both, individual and co-cultures, reaching approximately 1011 CFU/ml in all cases. These values were of 4.18 ± 0.24 IU/mg and 4.55 ± 0.29 IU/mg of xylanolytic activity at 48 h and 96 h, respectively, for Bacillus sp. AR03, while Paenibacillus sp. AR247 reached values of 0.59 ± 0.09 IU/mg and 0.40 ± 0.03 IU/mg at the same periods of cultivation. When mixtures (1:1) of the cell-free supernatant of individual cultures were assayed, it was observed that the enzymatic activity reached a maximum of 4.16 ± 0.39 IU/mg after 48 h of cultivation. This value was close to that obtained by the sum of the enzymatic activity of individual cultures, which was 4.77 IU/mg, for the same cultivation time. The obtained results were consistent with the observation of a synergistic effect on the degradation of xylan in the co-culture evaluated, with an estimated degree of synergism of 1.69 at 96 h. This synergy, which has been described for enzyme mixtures on industrial substrates, was observed here during the co-cultivation of Bacillus sp. AR03 and Paenibacillus sp. AR247. This system displayed a higher xylanolytic activity with respect to the individual cultivation of each isolate and a different zymographic pattern along the cultivation period. The obtained results of the xylanolytic activity for individual strains and the co-culture might indicate that the observed effect could not depend on an only addition of enzyme activities so that we may suggest the existence of a synergistic cooperation during the growth in the co-cultivation of the microorganism evaluated.Fil: Hero, Johan Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Pisa, José Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Perotti, Nora Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Romero, Cintia Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Martinez, Maria Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaXI Congreso Argentino de Microbiología GeneralCórdobaArgentinaAsociación Civil de Microbiología Genera

Tuning surface interactions on MgFe2O4 nanoparticles to induce interfacial hyperactivation in Candida rugosa lipase immobilization

Lipase adsorption on solid supports can be mediated by a precise balance of electrostatic and hydrophobic interactions. A suitable fine-tuning could allow the immobilized enzyme to display high catalytic activity. The objective of this work was to investigate how pH and ionic strength fluctuations affected protein-support interactions during immobilization via physical adsorption of a Candida rugosa lipase (CRL) on MgFe2O5. The highest amount of immobilized protein (IP) was measured at pH 4, and an ionic strength of 90 mM. However, these immobilization conditions did not register the highest hydrolytic activity (HA) in the biocatalyst (CRLa@MgFe2O4), finding the best values also at acidic pH but with a slight shift towards higher values of ionic strength around 110 mM. These findings were confirmed when the adsorption isotherms were examined under different immobilization conditions so that the maximum measurements of IP did not coincide with that of HA. Furthermore, when the recovered activity was examined, a strong interfacial hyperactivation of the lipase was detected towards acidic pH and highly charged surrounding environments. Spectroscopic studies, as well as in silico molecular docking analyses, revealed a considerable involvement of surface hydrophobic protein-carrier interactions, with aromatic aminoacids, especially phenylalanine residues, playing an important role. In light of these findings, this study significantly contributes to the body of knowledge and a better understanding of the factors that influence the lipase immobilization process on magnetic inorganic oxide nanoparticle surfaces.Fil: Morales, Andrés Hernán. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Hero, Johan Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Ledesma, Ana Estela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet Noa Sur. Centro de Investigación en Biofísica Aplicada y Alimentos. - Universidad Nacional de Santiago del Estero. Centro de Investigación en Biofísica Aplicada y Alimentos; ArgentinaFil: Martinez, Maria Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Navarro, María C.. Universidad Nacional de Tucuman. Facultad de Bioquímica, Química y Farmacia. Instituto de Química Inorganica. Cátedra de Química Inorganica; ArgentinaFil: Gómez, María I.. Universidad Nacional de Tucuman. Facultad de Bioquímica, Química y Farmacia. Instituto de Química Inorganica. Cátedra de Química Inorganica; ArgentinaFil: Romero, Cintia Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentin

Novel xylan degrading enzymes from polysaccharide utilizing loci of Prevotella copri DSM18205

Prevotella copri is a bacterium that can be found in the human gastrointestinal tract (GIT). The role of P. copri in the GIT is unclear, and elevated numbers of the microbe have been reported both in dietary fiber-induced improvement in glucose metabolism but also in conjunction with certain inflammatory conditions. These findings raised our interest in investigating the possibility of P. copri to grow on xylan, and identify the enzyme systems playing a role in digestion of xylan-based dietary fibers. Two xylan degrading polysaccharide utilizing loci (PUL10 and 15) were found in the genome, with three and eight glycoside hydrolase (GH) -encoding genes, respectively. Three of them were successfully produced in Escherichia coli: One extracellular enzyme from GH43 (subfamily 12, in PUL10, 60 kDa) and two enzymes from PUL15, one extracellular GH10 (41 kDa), and one intracellular GH43 (subfamily 137 kDa). Based on our results, we propose that in PUL15, GH10 (1) is an extracellular endo-1,4-β-xylanase, that hydrolazes mainly glucuronosylated xylan polymers to xylooligosaccharides (XOS); while, GH43_1 in the same PUL, is an intracellular β-xylosidase, catalyzing complete hydrolysis of the XOS to xylose. In PUL10, the characterized GH43_12 is an arabinofuranosidase, with a role in degradation of arabinoxylan, catalyzing removal of arabinose-residues on xylan.Fil: Linares Pastén, Javier A. Lund University. Biotechnology Department; SueciaFil: Hero, Johan Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Pisa, José Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Teixeira, Cristina. Lund University. Biotechnology Department; SueciaFil: Nyman, Margareta. Department Food Technology, Engineering And Nutrition; SueciaFil: Adlercreutz, Patrick. Lund University. Biotechnology Department; SueciaFil: Martinez, Maria Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Nordberg Karlsson, Eva. Universidad Nacional de Tucumán. Facultad de Ciencias Exactas y Tecnología; Argentin

Reading tea leaves worldwide: decoupled drivers of initial litter decomposition mass‐loss rate and stabilization

The breakdown of plant material fuels soil functioning and biodiversity. Currently, process understanding of global decomposition patterns and the drivers of such patterns are hampered by the lack of coherent large‐scale datasets. We buried 36,000 individual litterbags (tea bags) worldwide and found an overall negative correlation between initial mass‐loss rates and stabilization factors of plant‐derived carbon, using the Tea Bag Index (TBI). The stabilization factor quantifies the degree to which easy‐to‐degrade components accumulate during early‐stage decomposition (e.g. by environmental limitations). However, agriculture and an interaction between moisture and temperature led to a decoupling between initial mass‐loss rates and stabilization, notably in colder locations. Using TBI improved mass‐loss estimates of natural litter compared to models that ignored stabilization. Ignoring the transformation of dead plant material to more recalcitrant substances during early‐stage decomposition, and the environmental control of this transformation, could overestimate carbon losses during early decomposition in carbon cycle models

Improved development in magnetic Xyl-CLEAs technology for biotransformation of agro-industrial by-products through the use of a novel macromolecular cross-linker

Cross-Linked Enzyme Aggregates (CLEAs) technologies for enzyme immobilization are influenced by mass transference problems as the degree of molecular crosslinking achieved strongly affects the enzyme exposure to the substrates. Therefore, this work seeks to improve the accessibility of high molecular weight substrates by using macromolecular cross-linkers to the synthesis of a xylanolytic biocatalyst. After confirming that commercial polymers used as macromolecular cross-linkers significantly upgraded the xylanase activity from a crude preparation, a novel biopolymer/amyloid protein complex (BPAP) extracted from a microbial biofilm was used producing a remarkable recovery (83%) of the enzyme activity.A response surface methodology was applied to contrast the features of a previously developed biocatalyst with glutaraldehyde (GA@Xyl-CLEAs) and a novel one synthesized with BPAP combined with functionalized magnetic nanoparticles: mBPAP@Xyl-CLEAs. It was observed that the crosslinking agent used was the factor that most affected the enzyme activity. Also, the mBPAP system showed a similar and higher hydrolytic activity than those synthesized with GA, which was not affected by the mNPs/protein ratio. Finally, the mBPAP@Xyl-CLEAs were successfully tested for xylooligosaccharides production from agroindustrial-derived substrates, making this technology a promising practice to obtain green and suitable biocatalysts.Fil: Hero, Johan Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Morales, Andrés Hernán. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Perotti, Nora Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Romero, Cintia Mariana. Universidad Nacional de Tucuman. Facultad de Cs.exactas y Tecnología. Departamento de Ingeniería En Procesos y Gestion Industrial. Laboratorio de Biotecnología; ArgentinaFil: Martinez, Maria Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentin

Endoglucanase and xylanase production by Bacillus sp. AR03 in co-culture

The behavior of three isolates retrieved from different cellulolytic consortia, Bacillus sp. AR03, Paenibacillus sp. AR247 and Achromobacter sp. AR476-2, were examined individually and as co-cultures in order to evaluate their ability to produce extracellular cellulases and xylanases. Utilizing a peptone-based medium supplemented with carboxymethyl cellulose (CMC), an increase estimation of 1.30 and 1.50 times was obtained by the co-culture containing the strains AR03 and AR247, with respect to enzyme titles registered by their individual cultivation. On the contrary, the extracellular enzymatic production decreased during the co-cultivation of strain AR03 with the non-cellulolytic Achromobacter sp. AR476-2. The synergistic behavior observed through the combined cultivation of the strains AR03 and AR247 might be a consequence of the consumption by Paenibacillus sp. AR247 of the products of the CMC hydrolysis (i.e., cellobiose and/or cello-oligosaccharides), which were mostly generated by the cellulase producer Bacillus sp. AR03. The effect observed could be driven by the requirement to fulfill the nutritional supply from both strains on the substrate evaluated. These results would contribute to a better description of the degradation of the cellulose fraction of the plant cell walls in nature, expected to an efficient utilization of renewable sources.Fil: Hero, Johan Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; ArgentinaFil: Pisa, José Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; ArgentinaFil: Perotti, Nora Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; Argentina. Universidad Nacional de Tucumán; ArgentinaFil: Romero, Cintia Mariana. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; ArgentinaFil: Martinez, Maria Alejandra. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; Argentin

Impact of Prosopis nigra gum exudate in alginate core-shell beads synthesis by inverse gelation technique

The following work seeks to evaluate the impact of the polymer extracted from the gummy exudate of Prosopis nigra trees (PN-biopolymer, a carbohydrate polymer with protein moieties) in the inverse gelation technique for the oil encapsulation in alginate core-shell beads, as well as to contribute to the background reported in the different parameters that affect this process. The analysis of a complete factorial statistical design showed that the PN-biopolymer significantly affected all the responses evaluated, in principle generating stable high viscosity emulsions, reducing the deformation of the drop when entering the alginate bath, and promoting a more controlled calcium ions diffusion. Otherwise, unstable emulsions lead to great variability in the diameters and membrane thicknesses in the beads, generating unacceptable shapes. On the other hand, increases in CaCl2 concentration did not significantly affect the emulsion stability under the design conditions but negatively affected the sphericity of the beads. Besides, the membrane thickness was conditioned to the composition of the emulsion, so the Ca2+ ions complex with the negative charges of the PN-biopolymer, restricting their free diffusion according to the proportion of hydrocolloid involved in stabilizing the oil/water interface. The beads that produced the best results compromising all the responses studied were carried out at a PN-biopolymer concentration of 80% w/v, 1 M CaCl2, and an oil/water ratio of 0.25. This being the first report of the use of a gummy vegetable exudate in an inverse gelation process, PN-biopolymer constitutes a promising renewable natural candidate to develop encapsulates applicable to different industries.Fil: Morales, Andrés Hernán. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Spuches, Florencia Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Hero, Johan Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Alanís, Ana F.. Universidad Nacional de Tucumán; ArgentinaFil: Martinez, Maria Alejandra. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Romero, Cintia Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentin

Effect of the biological functionalization of nanoparticles on magnetic CLEA preparation

Lipase immobilization using adsorption on magnetic nanoparticles, cross-linked enzyme aggregates (CLEA), and a combination of both techniques was investigated. Experimental designs were used for the optimization of the immobilization observing that the pH and ionic strength play a principal role during the lipase immobilization and its activity. For adsorption on magnetic nanoparticles and CLEA synthesis the optimal condition was pH and 100 mM. Besides, during the CLEA synthesis, glutaraldehyde concentration showed to be a significant effect on the enzyme activity. A comparison between a magnetic CLEA prepared with (Lip@mCLEA) and without (mCLEA) biological functionalized magnetic nanoparticles was made observing that the use of functionalized support showed the best performance activity. All biocatalytic systems developed gives to the enzyme thermal stability between 45 and 70 °C, being Lip@mCLEA the more stable biocatalyst. Similar behavior was observed at different pH, where both Lip@mCLEA and mCLEA showed stability at a range of pH 5 to 8. The immobilized biocatalysts showed the same affinity of the subtract that the free enzyme suggested that the enzyme structure not modified the active site. The combination of both types of immobilization show evidenced the importance of the biological functionalization of the support when magnetic CLEA is produced.Fil: Abdulhamid, María Belén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; ArgentinaFil: Hero, Johan Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Zamora Luquez, Mariana. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; ArgentinaFil: Gómez, María Inés. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; ArgentinaFil: Navarro, Maria Carolina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química Inorgánica. Cátedra de Química General; ArgentinaFil: Romero, Cintia Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentin

Endo-xylanases from Cohnella sp. AR92 aimed at xylan and arabinoxylan conversion into value-added products

The genus Cohnella belongs to a group of Gram-positive endospore-forming bacteria within the Paenibacillaceae family. Although most species were described as xylanolytic bacteria, the literature still lacks some key information regarding their repertoire of xylan-degrading enzymes. The whole genome sequence of an isolated xylan-degrading bacterium Cohnella sp. strain AR92 was found to contain five genes encoding putative endo-1,4-β-xylanases, of which four were cloned, expressed, and characterized to better understand the contribution of the individual endo-xylanases to the overall xylanolytic properties of strain AR92. Three of the enzymes, CoXyn10A, CoXyn10C, and CoXyn11A, were shown to be effective at hydrolyzing xylans-derived from agro-industrial, producing oligosaccharides with substrate conversion values of 32.5%, 24.7%, and 10.6%, respectively, using sugarcane bagasse glucuronoarabinoxylan and of 29.9%, 19.1%, and 8.0%, respectively, using wheat bran-derived arabinoxylan. The main reaction products from GH10 enzymes were xylobiose and xylotriose, whereas CoXyn11A produced mostly xylooligosaccharides (XOS) with 2 to 5 units of xylose, often substituted, resulting in potentially prebiotic arabinoxylooligosaccharides (AXOS). The endo-xylanases assay displayed operational features (temperature optima from 49.9 to 50.4 °C and pH optima from 6.01 to 6.31) fitting simultaneous xylan utilization. Homology modeling confirmed the typical folds of the GH10 and GH11 enzymes, substrate docking studies allowed the prediction of subsites (− 2 to + 1 in GH10 and − 3 to + 1 in GH11) and identification of residues involved in ligand interactions, supporting the experimental data. Overall, the Cohnella sp. AR92 endo-xylanases presented significant potential for enzymatic conversion of agro-industrial by-products into high-value products. Key points • Cohnella sp. AR92 genome encoded five potential endo-xylanases. • Cohnella sp. AR92 enzymes produced xylooligosaccharides from xylan, with high yields. • GH10 enzymes from Cohnella sp. AR92 are responsible for the production of X2 and X3 oligosaccharides. • GH11 from Cohnella sp. AR92 contributes to the overall xylan degradation by producing substituted oligosaccharides. Graphical abstract: [Figure not available: see fulltext.]Fil: Hero, Johan Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Pisa, José Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Romero, Cintia Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; ArgentinaFil: Nordberg Karlsson, Eva. Lund University. Biotechnology Department; SueciaFil: Linares Pastén, Javier A.. Lund University. Biotechnology Department; SueciaFil: Martinez, Maria Alejandra. Universidad Nacional de Tucumán. Facultad de Ciencias Exactas y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentin