Characterization of a purified thermostable xylanase from Caldicoprobacter algeriensis sp. nov. strain TH7C1T

Bouanane‐Darenfed, Amel; Boucherba, Nawel; Bouacem, Khelifa; Gagaoua, Mohammed; Joseph, Manon; Kebbouche-Gana, Salima; Natèche, Farida; Hacène, Hocine; Ollivier, Bernard; Cayol, Jean‐Luc; Fardeau, Marie-Laure

doi:10.1016/j.carres.2015.10.013

Cited by 50 publications

(25 citation statements)

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“…Compost7_GH6 was highly tolerant to an alkaline environment, an essential characteristic for application in detergent industry [ 52 ]. Compost13_GH10 presented substrate specificity and hydrolysis profile of a typical endoxylanase [ 53 – 55 ]. In contrast, the enzyme compost21_GH11 presented a hydrolysis profile of a typical exo-enzyme, releasing xylobiose from xylan and xylooligosaccharides.…”

Section: Discussionmentioning

confidence: 99%

Targeted metatranscriptomics of compost-derived consortia reveals a GH11 exerting an unusual exo-1,4-β-xylanase activity

Mello

Alessi

Riaño‐Pachón

et al. 2017

Biotechnol Biofuels

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BackgroundUsing globally abundant crop residues as a carbon source for energy generation and renewable chemicals production stand out as a promising solution to reduce current dependency on fossil fuels. In nature, such as in compost habitats, microbial communities efficiently degrade the available plant biomass using a diverse set of synergistic enzymes. However, deconstruction of lignocellulose remains a challenge for industry due to recalcitrant nature of the substrate and the inefficiency of the enzyme systems available, making the economic production of lignocellulosic biofuels difficult. Metatranscriptomic studies of microbial communities can unveil the metabolic functions employed by lignocellulolytic consortia and identify novel biocatalysts that could improve industrial lignocellulose conversion.ResultsIn this study, a microbial community from compost was grown in minimal medium with sugarcane bagasse sugarcane bagasse as the sole carbon source. Solid-state nuclear magnetic resonance was used to monitor lignocellulose degradation; analysis of metatranscriptomic data led to the selection and functional characterization of several target genes, revealing the first glycoside hydrolase from Carbohydrate Active Enzyme family 11 with exo-1,4-β-xylanase activity. The xylanase crystal structure was resolved at 1.76 Å revealing the structural basis of exo-xylanase activity. Supplementation of a commercial cellulolytic enzyme cocktail with the xylanase showed improvement in Avicel hydrolysis in the presence of inhibitory xylooligomers.ConclusionsThis study demonstrated that composting microbiomes continue to be an excellent source of biotechnologically important enzymes by unveiling the diversity of enzymes involved in in situ lignocellulose degradation.Electronic supplementary materialThe online version of this article (10.1186/s13068-017-0944-4) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Targeted metatranscriptomics of compost-derived consortia reveals a GH11 exerting an unusual exo-1,4-β-xylanase activity

Mello

Alessi

Riaño‐Pachón

et al. 2017

Biotechnol Biofuels

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“…no. strain TH7C1 [ 46 ]. Thus the different concentrations of metal ions have variable effect on the xylanase activity, even for enzymes obtained from similar organism, and hence the metal ion concentration needs to be tightly regulated.…”

Section: Resultsmentioning

confidence: 99%

Thermostable Xylanase Production by Geobacillus sp. Strain DUSELR13, and Its Application in Ethanol Production with Lignocellulosic Biomass

2018

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The aim of the current study was to optimize the production of xylanase, and its application for ethanol production using the lignocellulosic biomass. A highly thermostable crude xylanase was obtained from the Geobacillus sp. strain DUSELR13 isolated from the deep biosphere of Homestake gold mine, Lead, SD. Geobacillus sp. strain DUSELR13 produced 6 U/mL of the xylanase with the beechwood xylan. The xylanase production was improved following the optimization studies, with one factor at a time approach, from 6 U/mL to 19.8 U/mL with xylan. The statistical optimization with response surface methodology further increased the production to 31 U/mL. The characterization studies revealed that the crude xylanase complex had an optimum pH of 7.0, with a broad pH range of 5.0–9.0, and an optimum temperature of 75 °C. The ~45 kDa xylanase protein was highly thermostable with t1/2 of 48, 38, and 13 days at 50, 60, and 70 °C, respectively. The xylanase activity increased with the addition of Cu+2, Zn+2, K+, and Fe+2 at 1 mM concentration, and Ca+2, Zn+2, Mg+2, and Na+ at 10 mM concentration. The comparative analysis of the crude xylanase against its commercial counterpart Novozymes Cellic HTec and Dupont, Accellerase XY, showed that it performed better at higher temperature, hydrolyzing 65.4% of the beechwood at 75 °C. The DUSEL R13 showed the mettle to hydrolyze, and utilize the pretreated, and untreated lignocellulosic biomass: prairie cord grass (PCG), and corn stover (CS) as the substrate, and gave a maximum yield of 20.5 U/mL with the untreated PCG. When grown in co-culture with Geobacillus thermoglucosidasius, it produced 3.53 and 3.72 g/L ethanol, respectively with PCG, and CS. With these characteristics the xylanase under study could be an industrial success for the high temperature bioprocesses.

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“…This is in accordance with the results of the xylanases from B. mojavensis A21 (Haddar et al 2012), G. mesophila KMM241 (Guo et al 2013), Geobacillus thermoleovorans (Verma and Satyanarayana 2012), M. cinnamomea (Fan et al 2014), etc. While some other xylanases showed xylosidase activity, the end product was xylose, such as originated from Thermoascus thermarum (Shi et al 2013), Thermoascus aurantiacus (Zhang et al 2011), the rumen contents of Hu sheep, and Caldicoprobacter algeriensis (Amel et al 2016). The hydrolysis properties could enable Xyn10A to be used as an effective and powerful enzyme for large-scale production of XOs, which can be used as prebiotics.…”

Section: Substrate Specificity and Analysis Of Hydrolytic Productsmentioning

confidence: 99%

“…They have been used widely in the conversion of lignocelluloses into fermentable sugars and prebiotic oligosaccharides (Juturu and Wu 2011;Shi et al 2013;Amel et al 2016). They can also be used to improve the quality of breads and beverages, enhance the digestibility of animal feeds, and improve the bleaching and deinking of paper (Huang et al 2006;Dhiman et al 2008;Garg et al 2009;Maity et al 2012;Singh et al 2012).…”

Section: Introductionmentioning

confidence: 99%

Characterization of a Salt-Tolerant and Cold-Adapted Xylanase from Bacillus cellulosilyticus

Sun

Shi

et al. 2016

BioResources

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A xylanase (Xyn10A) gene from the saline-alkali-tolerant microorganism Bacillus cellulosilyticus DSM 2522 was cloned and expressed in Escherichia coli BL21 (DE3). The open reading frame was composed of 1008 base pairs, and it encoded 335 amino acid residues belonging to glycosyl hydrolase family 10. The optimal temperature and pH of the purified Xyn10A were 40 °C and 8.0, respectively. The Xyn10A was sensitive to heat and showed obvious cold-adapted activity, retaining 38.3%, 55.7%, and 82.9% of the optimal activity at 4, 20, and 30 °C, respectively. Xyn10A also showed a high level of NaCl tolerance. The highest activity was observed with 1.5 M NaCl. The specific enzyme activity of Xyn10A was as much as 163.8 U/mg. Kinetic assays showed that Km, Vmax, and Kcat were 2.56 mg/mL, 202.5 μM/min/mg, and 132.6 /s, respectively. Additionally, the main hydrolysis products using birchwood xylan as substrate were xylobiose, xylotriose, and xylotetraose, as determined by thin layer chromatography analysis. As a cold-adapted and salt-tolerant enzyme, Xyn10A is an ideal candidate for further research and biotechnological applications.

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Characterization of a purified thermostable xylanase from Caldicoprobacter algeriensis sp. nov. strain TH7C1T

Cited by 50 publications

References 50 publications

Targeted metatranscriptomics of compost-derived consortia reveals a GH11 exerting an unusual exo-1,4-β-xylanase activity

Targeted metatranscriptomics of compost-derived consortia reveals a GH11 exerting an unusual exo-1,4-β-xylanase activity

Thermostable Xylanase Production by Geobacillus sp. Strain DUSELR13, and Its Application in Ethanol Production with Lignocellulosic Biomass

Characterization of a Salt-Tolerant and Cold-Adapted Xylanase from Bacillus cellulosilyticus

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