4.7 Article

Characterization of selenized polysaccharides from Ribes nigrum L. and its inhibitory effects on α-amylase and α-glucosidase

期刊

CARBOHYDRATE POLYMERS
卷 259, 期 -, 页码 -

出版社

ELSEVIER SCI LTD
DOI: 10.1016/j.carbpol.2021.117729

关键词

Ribes nigrum L.; Polysaccharides; Selenylation modification; alpha-Amylase and alpha-glucosidase; Mechanism

资金

  1. National Natural Science Foundation of China [31600276]
  2. Postdoctoral Scientific Research Startup Fund Project of Heilongjiang Province of China [LBH-Q19010]
  3. Student?s Innovation Training Program of Northeast Agricultural University [202010224351]

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The polysaccharide from Ribes nigrum L. was modified using nitric acid-sodium selenite method, resulting in selenized polysaccharides with improved water solubility and enzyme inhibition compared to the native polysaccharide. The selenized polysaccharides displayed reversible inhibition on two enzymes and formed complexes mainly driven by hydrophobic interactions and hydrogen bonding.
The polysaccharide from Ribes nigrum L. (RCP) was modified by nitric acid-sodium selenite method. After purification by Sepharose-6B, high purity native (PRCP) and three selenized polysaccharides (PRSPs) with different selenium contents were obtained. Compared with PRCP, PRSPs possessed the lower molecular weight, better water-solubility, physical stability and rheological properties. FT-IR and NMR spectra confirmed PRSPs had the characteristic absorption peaks of polysaccharides and the glycosidic bond types were not changed after selenylation modification, whereas the selenyl groups existing in PRSPs were mainly introduced at the C-6 position of sugar residue -> 4)-beta-D-Manp-(1 ->. Moreover, PRSPs displayed obviously smoother and smaller flaky structure than PRCP, and their inhibitory effects on alpha-amylase and alpha-glucosidase also were greater than PRCP. PRSPs exhibited a reversible inhibition on two enzymes in competitive manner and quenched their fluorescence through the static quenching mechanism. The polysaccharide-enzyme complex was spontaneously formed mainly driven by the hydrophobic interaction and hydrogen bonding.

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