Journal article
Substrate specificity of novel GH16 endo-β-(1→3)-galactanases acting on linear and branched β-(1→3)-1 galactooligosaccharides
Technical University of Denmark1
Enzyme Technology, Section for Protein Chemistry and Enzyme Technology, Department of Biotechnology and Biomedicine, Technical University of Denmark2
Section for Protein Chemistry and Enzyme Technology, Department of Biotechnology and Biomedicine, Technical University of Denmark3
Department of Biotechnology and Biomedicine, Technical University of Denmark4
Department of Chemistry, Technical University of Denmark5
Novozymes A/S6
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.
Language: | English |
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Year: | 2019 |
Pages: | 44-52 |
ISSN: | 18734863 and 01681656 |
Types: | Journal article |
DOI: | 10.1016/j.jbiotec.2018.12.006 |
ORCIDs: | Holck, Jesper , Enemark-Rasmussen, Kasper and Clausen, Mads Hartvig |