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Metformin-Induced Invertase Unfolding: Enzyme Kinetics and Activity Regulation
- Source :
- Journal of Agricultural and Food Chemistry; August 2024, Vol. 72 Issue: 32 p17977-17988, 12p
- Publication Year :
- 2024
-
Abstract
- The effects of metformin on invertase activity and its inhibition on sucrose digestion were studied. The rapid unfolding kinetics of invertases, followed a two-state model with an inactive intermediate formation. The dynamic interaction between metformin and invertase caused the secondary structure of the enzyme to become less β-sheet, more α-helix, and random coiling oriented, which weakened the binding force between enzyme and its substrate. Metformin acted as a chaotrope and disrupted the hydrogen bonds of water, which facilitated the unfolding of invertase. However, some sugar alcohols, which promoted the H-bond formation of water, could repair the secondary structure of metformin-denatured invertase and therefore regulate the enzyme activity. This research enriches our understanding of the mechanism of enzyme unfolding induced by guanidine compounds. Moreover, because metformin and sugar substitutes are of concern to diabetes, this research also provides useful information for understanding the activity of the digestive enzyme that coexists with metformin and sugar alcohols.
Details
- Language :
- English
- ISSN :
- 00218561 and 15205118
- Volume :
- 72
- Issue :
- 32
- Database :
- Supplemental Index
- Journal :
- Journal of Agricultural and Food Chemistry
- Publication Type :
- Periodical
- Accession number :
- ejs67051317
- Full Text :
- https://doi.org/10.1021/acs.jafc.4c03099