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Determining substrate specificities of β1,4-endo-galactanases using plant arabinogalactan oligosaccharides synthesized by automated glycan assembly

MPS-Authors
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Bartetzko,  Max Peter
Fabian Pfrengle, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Schuhmacher,  Frank
Peter H. Seeberger - Automated Systems, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Seeberger,  Peter H.
Peter H. Seeberger - Automated Systems, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Pfrengle,  Fabian
Fabian Pfrengle, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Fulltext (public)

Author_Manuscript.pdf
(Any fulltext), 857KB

Supplementary Material (public)

2383153_s.pdf
(Supplementary material), 6MB

Citation

Bartetzko, M. P., Schuhmacher, F., Seeberger, P. H., & Pfrengle, F. (2017). Determining substrate specificities of β1,4-endo-galactanases using plant arabinogalactan oligosaccharides synthesized by automated glycan assembly. The Journal of Organic Chemistry, 82(3), 1842-1850. doi:10.1021/acs.joc.6b02745.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002C-427E-F
Abstract
Pectin is a structurally complex plant polysaccharide with many industrial applications in food products. The structural elucidation of pectin is aided by digestion assays with glycosyl hydrolases. We report the automated glycan assembly of oligosaccharides related to the arabinogalactan side chains of pectin as novel biochemical tools to determine the substrate specificities of endo-galactanases. Analysis of the digestion products revealed different requirements for the lengths and arabinose substitution pattern of the oligosaccharides to be recognized and hydrolyzed by the galactanases.