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

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, en...

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Bibliographic Details
Published in:International journal of biological macromolecules 2020-11, Vol.162, p.1035-1043
Main Authors: Zhang, Mengshan, Zu, Heyang, Zhuang, Xumin, Yu, Yang, Wang, Yuan, Zhao, Zihan, Zhou, Yifa
Format: Article
Language:English
Subjects:
Apiaceae - chemistry
Galectin
Galectins - chemistry
Notopterygium incisum
Pectin
Pectins - chemistry
Pectins - isolation & purification
Plant Roots - chemistry
Polysaccharides
Structural analysis
UPLC-FLD-MSn
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Summary: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.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2020.06.216