Substrate specificity of novel GH16 endo-β-(1→3)-galactanases acting on linear and branched β-(1→3)-1 galactooligosaccharides

Panagiota Kalomoiri, Jesper Holck, Laure Coulomb, Irene Boos, Kasper Enemark-Rasmussen, Nikolaj Spodsberg, Rune Nygaard Monrad, Mads Hartvig Clausen*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

25 Downloads (Pure)

Abstract

Arabinogalactan proteins are proteoglycans located in the plant cell wall. Most arabinogalactan proteins are composed of carbohydrate moieties of β-(1→3)-galactan main chains with β-(1→6)-galactan side chains terminated by other glycans. In this study, three novel endo-β-(1→3)-galactanases were identified and the substrate specificity was further studied using well-defined galactan oligomers. Linear and branched β-(1→3)-linked galactans, which resemble the carbohydrate core of the arabinogalactan protein, were used for the characterization of endo-β-(1→3)-galactanases. The identified enzymes required at least three consecutive galactose residues for activity. Non-substituted regions were preferred, but substituents in the -2 and +2 and in some cases also -1 and +1 subsites were tolerated to some extent, depending on the branching pattern, however at a significantly lower rate/frequency.
Original languageEnglish
JournalJournal of Biotechnology
Volume290
Pages (from-to)44-52
ISSN0168-1656
DOIs
Publication statusPublished - 2019

Keywords

  • β-(1→3)-galactanases
  • Gum arabic
  • β-(1→3)-galactan
  • Type II arabinogalactan
  • Glycosyl hydrolase (GH) family 16

Cite this

@article{4bd1993024c84119b5dedfcf04ced9c8,
title = "Substrate specificity of novel GH16 endo-β-(1→3)-galactanases acting on linear and branched β-(1→3)-1 galactooligosaccharides",
abstract = "Arabinogalactan proteins are proteoglycans located in the plant cell wall. Most arabinogalactan proteins are composed of carbohydrate moieties of β-(1→3)-galactan main chains with β-(1→6)-galactan side chains terminated by other glycans. In this study, three novel endo-β-(1→3)-galactanases were identified and the substrate specificity was further studied using well-defined galactan oligomers. Linear and branched β-(1→3)-linked galactans, which resemble the carbohydrate core of the arabinogalactan protein, were used for the characterization of endo-β-(1→3)-galactanases. The identified enzymes required at least three consecutive galactose residues for activity. Non-substituted regions were preferred, but substituents in the -2 and +2 and in some cases also -1 and +1 subsites were tolerated to some extent, depending on the branching pattern, however at a significantly lower rate/frequency.",
keywords = "β-(1→3)-galactanases, Gum arabic, β-(1→3)-galactan, Type II arabinogalactan, Glycosyl hydrolase (GH) family 16",
author = "Panagiota Kalomoiri and Jesper Holck and Laure Coulomb and Irene Boos and Kasper Enemark-Rasmussen and Nikolaj Spodsberg and Monrad, {Rune Nygaard} and Clausen, {Mads Hartvig}",
year = "2019",
doi = "10.1016/j.jbiotec.2018.12.006",
language = "English",
volume = "290",
pages = "44--52",
journal = "Journal of Biotechnology",
issn = "0168-1656",
publisher = "Elsevier",

}

Substrate specificity of novel GH16 endo-β-(1→3)-galactanases acting on linear and branched β-(1→3)-1 galactooligosaccharides. / Kalomoiri, Panagiota ; Holck, Jesper; Coulomb, Laure; Boos, Irene; Enemark-Rasmussen, Kasper; Spodsberg, Nikolaj; Monrad, Rune Nygaard; Clausen, Mads Hartvig.

In: Journal of Biotechnology, Vol. 290, 2019, p. 44-52.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - Substrate specificity of novel GH16 endo-β-(1→3)-galactanases acting on linear and branched β-(1→3)-1 galactooligosaccharides

AU - Kalomoiri, Panagiota

AU - Holck, Jesper

AU - Coulomb, Laure

AU - Boos, Irene

AU - Enemark-Rasmussen, Kasper

AU - Spodsberg, Nikolaj

AU - Monrad, Rune Nygaard

AU - Clausen, Mads Hartvig

PY - 2019

Y1 - 2019

N2 - Arabinogalactan proteins are proteoglycans located in the plant cell wall. Most arabinogalactan proteins are composed of carbohydrate moieties of β-(1→3)-galactan main chains with β-(1→6)-galactan side chains terminated by other glycans. In this study, three novel endo-β-(1→3)-galactanases were identified and the substrate specificity was further studied using well-defined galactan oligomers. Linear and branched β-(1→3)-linked galactans, which resemble the carbohydrate core of the arabinogalactan protein, were used for the characterization of endo-β-(1→3)-galactanases. The identified enzymes required at least three consecutive galactose residues for activity. Non-substituted regions were preferred, but substituents in the -2 and +2 and in some cases also -1 and +1 subsites were tolerated to some extent, depending on the branching pattern, however at a significantly lower rate/frequency.

AB - Arabinogalactan proteins are proteoglycans located in the plant cell wall. Most arabinogalactan proteins are composed of carbohydrate moieties of β-(1→3)-galactan main chains with β-(1→6)-galactan side chains terminated by other glycans. In this study, three novel endo-β-(1→3)-galactanases were identified and the substrate specificity was further studied using well-defined galactan oligomers. Linear and branched β-(1→3)-linked galactans, which resemble the carbohydrate core of the arabinogalactan protein, were used for the characterization of endo-β-(1→3)-galactanases. The identified enzymes required at least three consecutive galactose residues for activity. Non-substituted regions were preferred, but substituents in the -2 and +2 and in some cases also -1 and +1 subsites were tolerated to some extent, depending on the branching pattern, however at a significantly lower rate/frequency.

KW - β-(1→3)-galactanases

KW - Gum arabic

KW - β-(1→3)-galactan

KW - Type II arabinogalactan

KW - Glycosyl hydrolase (GH) family 16

U2 - 10.1016/j.jbiotec.2018.12.006

DO - 10.1016/j.jbiotec.2018.12.006

M3 - Journal article

C2 - 30576682

VL - 290

SP - 44

EP - 52

JO - Journal of Biotechnology

JF - Journal of Biotechnology

SN - 0168-1656

ER -