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

Hero, Johan S. ; Pisa, José H. ; Romero, Cintia M. ; Nordberg Karlsson, Eva LU orcid ; Linares-Pastén, Javier A LU orcid and Martinez, M. Alejandra (2021) In Applied Microbiology and Biotechnology 105(18). p.6759-6778
Abstract

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... (More)

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.

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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
GH10, GH11, Cohnella sp. AR92, Xylooligosaccharides, Agro-industrial by-products, Molecular docking
in
Applied Microbiology and Biotechnology
volume
105
issue
18
pages
6759 - 6778
publisher
Springer
external identifiers
  • pmid:34458936
  • scopus:85114052002
ISSN
1432-0614
DOI
10.1007/s00253-021-11495-5
language
English
LU publication?
yes
id
9fd55f02-4aeb-4390-9bca-f4a0a41fda60
date added to LUP
2021-09-01 22:16:32
date last changed
2024-06-15 15:30:01
@article{9fd55f02-4aeb-4390-9bca-f4a0a41fda60,
  abstract     = {{<p>The genus <i>Cohnella </i>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 <i>Cohnella</i> sp. strain AR92 was found to contain five genes encoding putative endo-1,4-<i>β</i>-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 <i>Cohnella </i>sp. AR92 endo-xylanases presented significant potential for enzymatic conversion of agro-industrial by-products into high-value products.</p><p><b>Key points</b></p><p>• <i>Cohnella sp. AR92 genome encoded five potential endo-xylanases.</i></p><p><i>• Cohnella sp. AR92 enzymes produced xylooligosaccharides from xylan, with high yields.</i></p><p><i>• GH10 enzymes from Cohnella sp. AR92 are responsible for the production of X2 and X3 oligosaccharides.</i></p><p><i>• GH11 from Cohnella sp. AR92 contributes to the overall xylan degradation by producing substituted oligosaccharides.</i></p>}},
  author       = {{Hero, Johan S. and Pisa, José H. and Romero, Cintia M. and Nordberg Karlsson, Eva and Linares-Pastén, Javier A and Martinez, M. Alejandra}},
  issn         = {{1432-0614}},
  keywords     = {{GH10; GH11; Cohnella sp. AR92; Xylooligosaccharides; Agro-industrial by-products; Molecular docking}},
  language     = {{eng}},
  month        = {{08}},
  number       = {{18}},
  pages        = {{6759--6778}},
  publisher    = {{Springer}},
  series       = {{Applied Microbiology and Biotechnology}},
  title        = {{Endo-xylanases from <i>Cohnella</i> sp. AR92 aimed at xylan and arabinoxylan conversion into value-added products}},
  url          = {{http://dx.doi.org/10.1007/s00253-021-11495-5}},
  doi          = {{10.1007/s00253-021-11495-5}},
  volume       = {{105}},
  year         = {{2021}},
}