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

Linares-Pastén, Javier A LU orcid ; Hero, Johan Sebastian ; Pisa, José Horacio ; Teixeira, Cristina LU ; Nyman, Margareta LU ; Adlercreutz, Patrick LU orcid ; Martinez, M Alejandra and Karlsson, Eva Nordberg LU orcid (2021) In Glycobiology 31(10). p.1330-1349
Abstract

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... (More)

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.

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author
; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
arabinofuranosidase, polysaccharide utilizing loci, Prevotella copri, xylanase xylosidase
in
Glycobiology
volume
31
issue
10
pages
20 pages
publisher
Oxford University Press
external identifiers
  • pmid:34142143
  • scopus:85114568312
ISSN
1460-2423
DOI
10.1093/glycob/cwab056
language
English
LU publication?
yes
id
2c6fa3a9-3638-493c-8bd1-9e64baa81fa0
date added to LUP
2021-07-01 20:34:21
date last changed
2024-06-29 14:16:10
@article{2c6fa3a9-3638-493c-8bd1-9e64baa81fa0,
  abstract     = {{<p>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. </p>}},
  author       = {{Linares-Pastén, Javier A and Hero, Johan Sebastian and Pisa, José Horacio and Teixeira, Cristina and Nyman, Margareta and Adlercreutz, Patrick and Martinez, M Alejandra and Karlsson, Eva Nordberg}},
  issn         = {{1460-2423}},
  keywords     = {{arabinofuranosidase; polysaccharide utilizing loci; Prevotella copri; xylanase xylosidase}},
  language     = {{eng}},
  month        = {{10}},
  number       = {{10}},
  pages        = {{1330--1349}},
  publisher    = {{Oxford University Press}},
  series       = {{Glycobiology}},
  title        = {{Novel xylan-degrading enzymes from polysaccharide utilizing loci of Prevotella copri DSM18205}},
  url          = {{http://dx.doi.org/10.1093/glycob/cwab056}},
  doi          = {{10.1093/glycob/cwab056}},
  volume       = {{31}},
  year         = {{2021}},
}