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Arabinoxylanase from glycoside hydrolase family 5 is a selective enzyme for production of specific arabinoxylooligosaccharides

Falck, Peter LU ; Linares-Pastén, Javier LU orcid ; Nordberg Karlsson, Eva LU orcid and Adlercreutz, Patrick LU orcid (2018) In Food Chemistry 242. p.579-584
Abstract
An arabinose specific xylanase from glycoside hydrolase family 5 (GH5) was used to hydrolyse wheat and rye arabinoxylan, and the product profile showed that it produced arabinose substituted oligosaccharides (AXOS) having 2-10 xylose residues in the main chain but no unsubstituted xylooligosaccharides (XOS). Molecular modelling showed that the active site has an open structure and that the hydroxyl groups of all xylose residues in the active site are solvent exposed, indicating that arabinose substituents can be accommodated in the glycone as well as the aglycone subsites. The arabinoxylan hydrolysates obtained with the GH5 enzyme stimulated growth of Bifidobacterium adolescentis but not of Lactobacillus brevis. This... (More)
An arabinose specific xylanase from glycoside hydrolase family 5 (GH5) was used to hydrolyse wheat and rye arabinoxylan, and the product profile showed that it produced arabinose substituted oligosaccharides (AXOS) having 2-10 xylose residues in the main chain but no unsubstituted xylooligosaccharides (XOS). Molecular modelling showed that the active site has an open structure and that the hydroxyl groups of all xylose residues in the active site are solvent exposed, indicating that arabinose substituents can be accommodated in the glycone as well as the aglycone subsites. The arabinoxylan hydrolysates obtained with the GH5 enzyme stimulated growth of Bifidobacterium adolescentis but not of Lactobacillus brevis. This arabinoxylanase is thus a good tool for the production of selective prebiotics. (Less)
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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Xylanase, Prebiotics, Oligosaccharides, Bifidobacterium
in
Food Chemistry
volume
242
pages
579 - 584
publisher
Elsevier
external identifiers
  • scopus:85030107844
  • wos:000413291700076
  • pmid:29037732
ISSN
0308-8146
DOI
10.1016/j.foodchem.2017.09.048
project
ANTIDIABETIC FOOD CENTRE
language
English
LU publication?
yes
id
6791f457-e69b-437d-81b9-7d8d3ad74376
date added to LUP
2017-09-22 05:41:56
date last changed
2022-04-01 19:34:52
@article{6791f457-e69b-437d-81b9-7d8d3ad74376,
  abstract     = {{An arabinose specific xylanase from glycoside hydrolase family 5 (GH5) was used to hydrolyse wheat and rye arabinoxylan, and the product profile showed that it produced arabinose substituted oligosaccharides (AXOS) having 2-10 xylose residues in the main chain but no unsubstituted xylooligosaccharides (XOS). Molecular modelling showed that the active site has an open structure and that the hydroxyl groups of all xylose residues in the active site are solvent exposed, indicating that arabinose substituents can be accommodated in the glycone as well as the aglycone subsites. The arabinoxylan hydrolysates obtained with the GH5 enzyme stimulated growth of <i>Bifidobacterium adolescentis</i> but not of <i>Lactobacillus brevis</i>. This arabinoxylanase is thus a good tool for the production of selective prebiotics.}},
  author       = {{Falck, Peter and Linares-Pastén, Javier and Nordberg Karlsson, Eva and Adlercreutz, Patrick}},
  issn         = {{0308-8146}},
  keywords     = {{Xylanase; Prebiotics; Oligosaccharides; Bifidobacterium}},
  language     = {{eng}},
  pages        = {{579--584}},
  publisher    = {{Elsevier}},
  series       = {{Food Chemistry}},
  title        = {{Arabinoxylanase from glycoside hydrolase family 5 is a selective enzyme for production of specific arabinoxylooligosaccharides}},
  url          = {{http://dx.doi.org/10.1016/j.foodchem.2017.09.048}},
  doi          = {{10.1016/j.foodchem.2017.09.048}},
  volume       = {{242}},
  year         = {{2018}},
}