Polymerization

Biology

Pectin

Biochemistry

Arabinogalactan

Food science

Polysaccharide

Stereochemistry

Immunology

Polymer

Avidity

Organic chemistry

Toxicology

Galectin

Enzyme

Hydrolysis

Chemistry

Enzymatic hydrolysis

Degree of polymerization

Antibody

International Journal of Biological Macromolecules

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.

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