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

Hero, Johan S.; Pisa, José Horacio; Romero, Cintia Mariana; Karlsson, Eva Nordberg; Linares-Pastén, Javier A.; Martinez, María Alejandra

doi:10.1007/s00253-021-11495-5

Cited by 5 publications

(6 citation statements)

References 96 publications

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“…Compared with acid hydrolysis and auto-hydrolytic processes, enzymatic hydrolysis has particular advantages including less harsh conditions, higher efficiency and specificity, better control over the product’s degree of polymerization (DP), and more functional XOS yields [ 5 ]. In enzymatic hydrolysis, endo-β-1,4-xylanase (EC 3.2.1.8) is a rate-limiting enzyme, which randomly catalyzes the hydrolysis of β-1,4 xylose linkages in the backbone and yields XOS with various DP [ 6 , 7 ]. To date, endo-1,4-β-xylanase was classified into the glycoside hydrolases (GH) 5, 8, 10, 11, and 43 based on amino acid sequence homology comparison [ 8 ].…”

Section: Introductionmentioning

confidence: 99%

Crucial Residues of C-Terminal Oligopeptide C60 to Improve the Yield of Prebiotic Xylooligosaccharides by Truncated Mutation

Pan

Jin

Wang

et al. 2022

Foods

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Increasing the yields of short xylooligosaccharides by enzymatic production is efficient to improve prebiotic effects. Previously, C-terminal oligopeptide C60 was found to accelerate short xylooligosaccharides. Herein, in order to further understand the molecular mechanism of C60, the sequence analysis firstly showed that C60 displays typical properties of a linker (rich in proline/alanine/glycine/glutamine/arginine, 8.33–20.00%). C60 shared the highest identity with the N-terminal region of esterase (98.33%) and high identity with the linker between xylanase and esterase from Prevotella sp. (56.50%), it is speculated to originate from an early linker between XynA and another domain. Besides, structure simulation showed that C60 enhances the molecular interactions between substrate and active residues to improve catalytic efficiency. Moreover, three truncated variants with different lengths of C-terminal regions were successfully generated in Escherichia coli. The specific activities of variants were 6.44–10.24 fold of that of XynA-Tr, and their optimal temperature and pH were the same as XynA-Tr. Three truncated variants released more xylooligosaccharides, especially xylobiose (46.33, 43.41, and 49.60%), than XynA-Tr (32.43%). These results are helpful to understand the molecular mechanism of C60, and also provide new insight to improve the yields of short xylooligosaccharides by molecular modification at the terminal of xylanases.

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Section: Introductionmentioning

confidence: 99%

Crucial Residues of C-Terminal Oligopeptide C60 to Improve the Yield of Prebiotic Xylooligosaccharides by Truncated Mutation

Pan

Jin

Wang

et al. 2022

Foods

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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%

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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“…A hypothetical model for xylan utilization by AR92 strain is proposed based on the genomic and proteomic assessment performed (Figure 4). Accordingly, at least six endo‐β‐xylanases belonging GH10 and GH11 families were identified as probable tools to reduce the polymerization degree of xylan backbone, releasing varied xylooligomer sizes by this microorganism (Hero et al, 2021; Pisa et al, 2017). The redundancy of such enzymes was observed in other bacterial strains able to degrade complex polysaccharides from vegetal biomass.…”

Section: Resultsmentioning

confidence: 99%

A genome–proteome‐based approach for xylan degradation by Cohnella sp. AR92

Pisa

Hero

Romero

et al. 2022

Environ Microbiol Rep

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Several members of Cohnella genus have been reported as xylanolytic bacteria with significant capacity as carbohydrate-active enzyme producers (CAZymes), whose mechanisms involving xylan degradation are a key goal for suitable applications in bio-based industries. Using Cohnella sp. AR92 bacterium, we ensembled a genomic-proteomic approach to assess plant biomass conversion targeting its xylanolytic set of enzymes. Also, the genomic traits of the strain AR92 were compared to other Cohnella spp., showing a significant variability in terms of genome sizes and content of genes that code CAZymes. The AR92 strain genome harbours 209 CAZymes encoding sequences active on different polysaccharides, particularly directed towards xylans. Concurrent proteomic data recovered from cultures containing three kinds of lignocellulosic-derived substrates showed a broad set of xylan-degrading enzymes. The most abundant CAZymes expressed in the different conditions assayed were endo-β-1,4-xylanases belonging to the GH11 and GH10 families, enzymes that were previously proved to be useful in the biotransformation of lignocellulosic biomass derived from sugarcane as well as onto xylan-enriched substrates. Therefore, considering the large reserve of CAZymes of Cohnella sp. AR92, a xylan processing model for AR92 strain is proposed.

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

Cited by 5 publications

References 96 publications

Crucial Residues of C-Terminal Oligopeptide C60 to Improve the Yield of Prebiotic Xylooligosaccharides by Truncated Mutation

Crucial Residues of C-Terminal Oligopeptide C60 to Improve the Yield of Prebiotic Xylooligosaccharides by Truncated Mutation

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

A genome–proteome‐based approach for xylan degradation by Cohnella sp. AR92

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