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Endo-xylanases as tools for production of substituted xylooligosaccharides with prebiotic properties

Nordberg Karlsson, Eva LU ; Schmitz, Eva LU ; Linares-Pastén, Javier A. LU and Adlercreutz, Patrick LU (2018) In Applied Microbiology and Biotechnology 102(21). p.9081-9088
Abstract

Xylan has a main chain consisting of β-1,4-linked xylose residues with diverse substituents. Endoxylanases cleave the xylan chain at cleavage sites determined by the substitution pattern and thus give different oligosaccharide product patterns. Most known endoxylanases belong to glycoside hydrolase (GH) families 10 and 11. These enzymes work well on unsubstituted xylan but accept substituents in certain subsites. The GH11 enzymes are more restricted by substituents, but on the other hand, they are normally more active than the GH10 enzymes on insoluble substrates, because of their smaller size. GH5 endoxylanases accept arabinose substituents in several subsites and require it in the − 1 subsite. This specificity makes the GH5... (More)

Xylan has a main chain consisting of β-1,4-linked xylose residues with diverse substituents. Endoxylanases cleave the xylan chain at cleavage sites determined by the substitution pattern and thus give different oligosaccharide product patterns. Most known endoxylanases belong to glycoside hydrolase (GH) families 10 and 11. These enzymes work well on unsubstituted xylan but accept substituents in certain subsites. The GH11 enzymes are more restricted by substituents, but on the other hand, they are normally more active than the GH10 enzymes on insoluble substrates, because of their smaller size. GH5 endoxylanases accept arabinose substituents in several subsites and require it in the − 1 subsite. This specificity makes the GH5 endoxylanases very useful for degradation of highly arabinose-substituted xylans and for the selective production of arabinoxylooligosaccharides, without formation of unsubstituted xylooligosaccharides. The GH30 endoxylanases have a related type of specificity in that they require a uronic acid substituent in the − 2 subsite, which makes them very useful for the production of uronic acid substituted oligosaccharides. The ability of dietary xylooligosaccharides to function as prebiotics in humans is governed by their substitution patterns. Endoxylanases are thus excellent tools to tailor prebiotic oligosaccharides to stimulate various types of intestinal bacteria and to cause fermentation in different parts of the gastrointestinal tract. Continuously increasing knowledge on the function of the gut microbiota and discoveries of novel endoxylanases increase the possibilities to achieve health-promoting effects.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Arabinose, Oligosaccharide, Prebiotics, Uronic acids, Xylanase
in
Applied Microbiology and Biotechnology
volume
102
issue
21
pages
9081 - 9088
publisher
Springer
external identifiers
  • scopus:85053026736
  • pmid:30196329
ISSN
0175-7598
DOI
10.1007/s00253-018-9343-4
language
English
LU publication?
yes
id
828aa8a6-42df-4f21-b1d1-c064b32b5c1b
date added to LUP
2018-10-09 01:27:56
date last changed
2020-01-22 07:15:18
@article{828aa8a6-42df-4f21-b1d1-c064b32b5c1b,
  abstract     = {<p>Xylan has a main chain consisting of β-1,4-linked xylose residues with diverse substituents. Endoxylanases cleave the xylan chain at cleavage sites determined by the substitution pattern and thus give different oligosaccharide product patterns. Most known endoxylanases belong to glycoside hydrolase (GH) families 10 and 11. These enzymes work well on unsubstituted xylan but accept substituents in certain subsites. The GH11 enzymes are more restricted by substituents, but on the other hand, they are normally more active than the GH10 enzymes on insoluble substrates, because of their smaller size. GH5 endoxylanases accept arabinose substituents in several subsites and require it in the − 1 subsite. This specificity makes the GH5 endoxylanases very useful for degradation of highly arabinose-substituted xylans and for the selective production of arabinoxylooligosaccharides, without formation of unsubstituted xylooligosaccharides. The GH30 endoxylanases have a related type of specificity in that they require a uronic acid substituent in the − 2 subsite, which makes them very useful for the production of uronic acid substituted oligosaccharides. The ability of dietary xylooligosaccharides to function as prebiotics in humans is governed by their substitution patterns. Endoxylanases are thus excellent tools to tailor prebiotic oligosaccharides to stimulate various types of intestinal bacteria and to cause fermentation in different parts of the gastrointestinal tract. Continuously increasing knowledge on the function of the gut microbiota and discoveries of novel endoxylanases increase the possibilities to achieve health-promoting effects.</p>},
  author       = {Nordberg Karlsson, Eva and Schmitz, Eva and Linares-Pastén, Javier A. and Adlercreutz, Patrick},
  issn         = {0175-7598},
  language     = {eng},
  month        = {09},
  number       = {21},
  pages        = {9081--9088},
  publisher    = {Springer},
  series       = {Applied Microbiology and Biotechnology},
  title        = {Endo-xylanases as tools for production of substituted xylooligosaccharides with prebiotic properties},
  url          = {http://dx.doi.org/10.1007/s00253-018-9343-4},
  doi          = {10.1007/s00253-018-9343-4},
  volume       = {102},
  year         = {2018},
}