Arabinoxylanase from glycoside hydrolase family 5 is a selective enzyme for production of specific arabinoxylooligosaccharides
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/6791f457-e69b-437d-81b9-7d8d3ad74376
- author
- Falck, Peter LU ; Linares-Pastén, Javier LU ; Nordberg Karlsson, Eva LU and Adlercreutz, Patrick LU
- organization
- publishing date
- 2018
- 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}}, }