Inhibitory effects of a low-molecular-weight sulfated fucose-containing saccharide on α-amylase and α-glucosidase prepared from ascophyllan. Issue 3 (12th January 2022)
- Record Type:
- Journal Article
- Title:
- Inhibitory effects of a low-molecular-weight sulfated fucose-containing saccharide on α-amylase and α-glucosidase prepared from ascophyllan. Issue 3 (12th January 2022)
- Main Title:
- Inhibitory effects of a low-molecular-weight sulfated fucose-containing saccharide on α-amylase and α-glucosidase prepared from ascophyllan
- Authors:
- Zhan, Hui
Yu, Gang
Zheng, Mingjing
Zhu, Yanbing
Ni, Hui
Oda, Tatsuya
Jiang, Zedong - Abstract:
- Abstract : A low-molecular-weight sulfated fucose-containing saccharide with potent inhibition on α-glucosidase but mild inhibition on α-amylase was prepared from alginate lyase digested ascophyllan, having desirable characteristics as an anti-diabetic agent. Abstract : To find natural and safe anti-diabetic foods or potential drugs, low-molecular-weight saccharide fragments LMWAs-H ( M w 33.48 kDa) and LMWAs-L ( M w 6.71 kDa) from the sulfated polysaccharide ascophyllan of Ascophyllum nodosum using alginate lyase (EC 4.2.2.3) were investigated. The results revealed that LMWAs-H possessed potent inhibition activity against α-glucosidase or α-amylase in a concentration-dependent manner, which were higher than native ascophyllan or LMWAs-L. LMWAs-H exhibited a stronger inhibitory activity against α-glucosidase than α-amylase because it differently affects the conformational structures of these enzymes. Structural analysis revealed LMWAs-H to be →4)-α-l -Fuc p -(1 → 4)-α-l -Fuc p -(1 → 3)-β-d -Xyl p -(1 → 3)-α-l -Fuc p 4S(1→ as main chain, and T -α-d -Glc p -(1→ and →3)-β-d -Man p Ared residues were attached to the ends of main chain as non-reducing- and reducing-end residues, respectively. The 4-deoxy-l - erythro -hex-4-enuronosyluronate linked the O-4 position of →3, 4)-β-d -ManpAred residue as side branches. Our results suggest that LMWAs-H is the main active structural motif responsible for the enzymes-inhibiting activities, which is probably derived from theAbstract : A low-molecular-weight sulfated fucose-containing saccharide with potent inhibition on α-glucosidase but mild inhibition on α-amylase was prepared from alginate lyase digested ascophyllan, having desirable characteristics as an anti-diabetic agent. Abstract : To find natural and safe anti-diabetic foods or potential drugs, low-molecular-weight saccharide fragments LMWAs-H ( M w 33.48 kDa) and LMWAs-L ( M w 6.71 kDa) from the sulfated polysaccharide ascophyllan of Ascophyllum nodosum using alginate lyase (EC 4.2.2.3) were investigated. The results revealed that LMWAs-H possessed potent inhibition activity against α-glucosidase or α-amylase in a concentration-dependent manner, which were higher than native ascophyllan or LMWAs-L. LMWAs-H exhibited a stronger inhibitory activity against α-glucosidase than α-amylase because it differently affects the conformational structures of these enzymes. Structural analysis revealed LMWAs-H to be →4)-α-l -Fuc p -(1 → 4)-α-l -Fuc p -(1 → 3)-β-d -Xyl p -(1 → 3)-α-l -Fuc p 4S(1→ as main chain, and T -α-d -Glc p -(1→ and →3)-β-d -Man p Ared residues were attached to the ends of main chain as non-reducing- and reducing-end residues, respectively. The 4-deoxy-l - erythro -hex-4-enuronosyluronate linked the O-4 position of →3, 4)-β-d -ManpAred residue as side branches. Our results suggest that LMWAs-H is the main active structural motif responsible for the enzymes-inhibiting activities, which is probably derived from the fucose-containing branches of ascophyllan. Our findings reveal that the strong inhibition of LMWAs-H on α-glucosidase but mild inhibition on α-amylase is highly related to its structural properties, suggesting its desirable characteristics as an anti-diabetic agent. … (more)
- Is Part Of:
- Food & function. Volume 13:Issue 3(2022)
- Journal:
- Food & function
- Issue:
- Volume 13:Issue 3(2022)
- Issue Display:
- Volume 13, Issue 3 (2022)
- Year:
- 2022
- Volume:
- 13
- Issue:
- 3
- Issue Sort Value:
- 2022-0013-0003-0000
- Page Start:
- 1119
- Page End:
- 1132
- Publication Date:
- 2022-01-12
- Subjects:
- Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
Nutrition -- Periodicals
664.07 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/FO ↗
http://pubs.rsc.org/en/journals/journal/fo ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d1fo03331j ↗
- Languages:
- English
- ISSNs:
- 2042-6496
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.038457
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 20738.xml