Characterization of selenized polysaccharides from Ribes nigrum L. and its inhibitory effects on α-amylase and α-glucosidase. (1st May 2021)

• Record Type: Journal Article
• Authors: Zhao, Meimei; Bai, Jingwen; Bu, Xueying; Yin, Yuting; Wang, Libo; Yang, Yu; Xu, Yaqin
• Is Part Of: Carbohydrate polymers. Volume 259(2021)
• Publication Date: 2021-05-01
• Subjects: Ribes nigrum L. -- Polysaccharides -- Selenylation modification -- α-Amylase and α-glucosidase -- Mechanism; Polysaccharides -- Periodicals; Polysaccharides -- Periodicals; Polysaccharides -- Périodiques; Electronic journals; 547.78
• DOI: 10.1016/j.carbpol.2021.117729
• Languages: English
• ISSNs: 0144-8617

Abstract

Graphical abstract: Highlights: Three selenized polysaccharides from Ribes nigrum L. were successfully prepared. The main skeleton structure of PRCP was not changed after selenylation modification. PRSPs showed lower M w, better physicochemical and rheological properties than PRCP. PRSPs and PRCP were reversible and competitive inhibitor on α -amylase/ α -glucosidase. The inhibition of PRSPs and PRCP on α -amylase/ α -glucosidase was the static quenching. Abstract: 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)- β -d -Manp-(1→. Moreover, PRSPs displayed obviously smoother and smaller flaky structure than PRCP, and their inhibitory effects on α -amylase and α -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.