Novel xylan-degrading enzymes from polysaccharide utilizing loci of Prevotella copri DSM18205
(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.
(Less)
- author
- Linares-Pastén, Javier A
LU
; Hero, Johan Sebastian ; Pisa, José Horacio ; Teixeira, Cristina LU ; Nyman, Margareta LU ; Adlercreutz, Patrick LU
; Martinez, M Alejandra and Karlsson, Eva Nordberg LU
- organization
- publishing date
- 2021-10-01
- 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}}, }