Production of prebiotic xylooligosaccharides from arabino- and glucuronoxylan using a two-domain Jonesia denitrificans xylanase from GH10 family

Vacilotto, Milena Moreira; Sepulchro, Ana Gabriela Veiga; Pellegrini, Vanessa de Oliveira Arnoldi; Polikarpov, Igor

doi:10.1016/j.enzmictec.2021.109743

Cited by 10 publications

(3 citation statements)

References 46 publications

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“…Xyl10B presented higher specific activity values (255 IU/mg) than other GH10 xylanases identified from metagenomics analyses, such as: Pm25, derived from the (Jacomini et al 2020;Hero et al 2021;Vacilotto et al 2021). On the other hand, it showed an activity range similar to that of rXylR from Duganella sp.…”

Section: Discussionmentioning

confidence: 80%

“…As compared with xylanases derived from bacteria, Xyl10B showed higher specific activity than some of them, such as JdXyn10A, derived from Jonesia denitrificans (~ 65 IU/mg), CoXyn10A, derived from Cohnella sp. (~ 71.16 IU/mg), and XynA2, derived from Caulobacter crescentus (~ 1.02 IU/mg) (Jacomini et al 2020 ; Hero et al 2021 ; Vacilotto et al 2021 ). On the other hand, it showed an activity range similar to that of rXylR from Duganella sp.…”

Section: Discussionmentioning

confidence: 99%

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Characterization of a novel GH10 alkali-thermostable xylanase from a termite microbiome

Mon

Villegas

Campos

et al. 2022

Bioresour. Bioprocess.

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The aim of the present study was to assess the biochemical and molecular structural characteristics of a novel alkali-thermostable GH10 xylanase (Xyl10B) identified in a termite gut microbiome by a shotgun metagenomic approach. This endoxylanase candidate was amplified, cloned, heterologously expressed in Escherichia coli and purified. The recombinant enzyme was active at a broad range of temperatures (37–60 ºC) and pH values (4–10), with optimal activity at 50 ºC and pH 9. Moreover, its activity remained at more than 80% of its maximum at 50 °C for 8 h. In addition, Xyl10B was found to be stable in the presence of salt and several ions and chemical reagents frequently used in the industry. These characteristics make this enzyme an interesting candidate for pulp and paper bleaching industries, since this process requires enzymes without cellulase activity and resistant to high temperatures and alkaline pH (thermo-alkaliphilic enzymes). The products of xylan hydrolysis by Xyl10B (short xylooligosaccharides, xylose and xylobiose) could be suitable for application as prebiotics and in the production of bioethanol. Graphical Abstract

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Section: Discussionmentioning

confidence: 80%

Section: Discussionmentioning

confidence: 99%

Characterization of a novel GH10 alkali-thermostable xylanase from a termite microbiome

Mon

Villegas

Campos

et al. 2022

Bioresour. Bioprocess.

View full text Add to dashboard Cite

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“…niveu, as well as over bacteria such as Thermobacillus composti, Paludibacter propionicigenes, and Streptomyces sp. B6 [36][37][38][39][40][41]. XynST7 has better pH stability and thermostability than others, while XynST7 utilized xylan to produce XOS and no xylose, which may be of benefit during XOS purification (Table 3).…”

Section: Xos Productionmentioning

confidence: 99%

Identification and Characterization of a Novel Endo-β-1,4-Xylanase from Streptomyces sp. T7 and Its Application in Xylo-Oligosaccharide Production

Zhang

et al. 2022

Molecules

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A xylanase-producing strain, identified as Streptomyces sp. T7, was isolated from soil by our lab. The endo-β-1,4-xylanase (xynST7) gene was found in the genome sequence of strain T7, which was cloned and expressed in Escherichia coli. XynST7 belonged to the glycoside hydrolase family 10, with a molecular mass of approximately 47 kDa. The optimum pH and temperature of XynST7 were pH 6.0 and 60 °C, respectively, and it showed wide pH and temperature adaptability and stability, retaining more than half of its enzyme activity between pH 5.0 and 11.0 below 80 °C. XynST7 showed only endo-β-1,4-xylanase activity without cellulase- or β-xylosidase activity, and it showed maximal hydrolysis for corncob xylan in all the test substrates. Then, XynST7 was used for the production of xylo-oligosaccharides (XOSs) by hydrolyzing xylan extracted from raw corncobs. The maximum yield of the XOS was 8.61 ± 0.13 mg/mL using 15 U/mL of XynST7 and 1.5% corncob xylan after 10 h of incubation at 60 °C. The resulting hydrolysate products mainly consisted of xylobiose and xylotriose. These data indicated that XynST7 might by a promising tool for various industrial applications.

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Recent advances in the enzymatic production and applications of xylooligosaccharides

Capetti

Vacilotto

Dabul

et al. 2021

World J Microbiol Biotechnol

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Production of prebiotic xylooligosaccharides from arabino- and glucuronoxylan using a two-domain Jonesia denitrificans xylanase from GH10 family

Cited by 10 publications

References 46 publications

Characterization of a novel GH10 alkali-thermostable xylanase from a termite microbiome

Characterization of a novel GH10 alkali-thermostable xylanase from a termite microbiome

Identification and Characterization of a Novel Endo-β-1,4-Xylanase from Streptomyces sp. T7 and Its Application in Xylo-Oligosaccharide Production

Recent advances in the enzymatic production and applications of xylooligosaccharides

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