Structural analyses of the HG-type pectin from notopterygium incisum and its effects on galectins.

Published on Nov 1, 2020in International Journal of Biological Macromolecules5.162
· DOI :10.1016/J.IJBIOMAC.2020.06.216
Mengshan Zhang4
Estimated H-index: 4
(Northeast Normal University),
Heyang Zu1
Estimated H-index: 1
(Northeast Normal University)
+ 4 AuthorsYifa Zhou29
Estimated H-index: 29
(Northeast Normal University)
Abstract In the manuscript, water-soluble polysaccharides WPNI was extracted from notopterygium incisum roots and separated into two homogeneous fractions WPNI-A-a and WPNI-A-b. WPNI-A-a was an arabinogalactan (AG). WPNI-A-b belonged to HG type pectin. The structure of WPNI-A-b was analyzed by FT-IR, NMR, enzymatic hydrolysis (Endo-PG) and UPLC-FLD-MSn. WPNI-A-b was dominated by HG domain, covalently linked with AG and RG-II domains. Oligogalacturonides produced by Endo-PG from HG domain were non-, mono-, di- or tri-methyl esterified with degree of polymerization (DP) from 1 to 6. The distribution of methyl-ester groups was in a block wise manner. The interaction of WPNI-A-b and its enzymatic hydrolysis products with galectin-1, galectin-3, galectin-7 and galectin-8 showed that AG domain exhibited stronger binding avidity to galectins than RG-II and HG domain, while oligogalacturonides showed no binding activities to galectins. The results would be useful for the application of the pectin from notopterygium incisum.
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