Loading…
Structural characterization and hypolipidemic activity of Gracilaria lemaneiformis polysaccharide and its degradation products
•The effect of H2O2-Vc degradation on Gracilaria lemaneiformis polysaccharide.•The structures of Gracilaria lemaneiformis polysaccharide and oligosaccharide were studied.•The inhibitory effects on pancreatic lipase and cholesterol esterase were analyzed.•The relationship of structure and hypolipidem...
Saved in:
Published in: | Food Chemistry: X 2022-06, Vol.14, p.100314-100314, Article 100314 |
---|---|
Main Authors: | , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | •The effect of H2O2-Vc degradation on Gracilaria lemaneiformis polysaccharide.•The structures of Gracilaria lemaneiformis polysaccharide and oligosaccharide were studied.•The inhibitory effects on pancreatic lipase and cholesterol esterase were analyzed.•The relationship of structure and hypolipidemic activity was revealed.
This research aimed to analyze structural characterization and hypolipidemic activity in vitro of G. lemaneiformis polysaccharide (GLP) and its degradation products. The results presented that the content of galacturonic acid declined and glucuronic acid level enhanced, average particle size decreased from 99.9 μm to 25.7 μm, and color brightness of polysaccharide strengthened after degraded by H2O2-Vc. There was no significant change in thermal stability of polysaccharide before and after degradation. It was observed in AFM analysis, polysaccharide changed to smaller, delicacy and dispersion after degradation. As seen in FT-IR, H2O2-Vc degradation never change the structure of polysaccharide. Polysaccharide and its degradation products showed a significant inhibition effect on pancreatic lipase and cholesterol esterase in a dose-dependent manner, which presented the mixed type of competitive and non-competitive for pancreatic lipase, and non-competitive for cholesterol esterase, respectively. The fluorescence quenching type was static on pancreatic lipase and dynamic on cholesterol esterase. |
---|---|
ISSN: | 2590-1575 2590-1575 |
DOI: | 10.1016/j.fochx.2022.100314 |