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Changes of porcine pancreas α-amylase in activity and secondary conformations under inhibition of tea polyphenols.

Authors :
Liu, Shumin
Ou, Shiyi
Huang, Huihua
Source :
International Journal of Food Science & Technology. Jun2016, Vol. 51 Issue 6, p1537-1543. 7p.
Publication Year :
2016

Abstract

To investigate two-sided functions of tea polyphenols ( TP) in antinutrition and energy balance modulation, TP were extracted from Chinese green tea and used to complex porcine pancreas α-amylase ( PPA). Changes of PPA in activity and secondary conformations were analysed. Porcine pancreas α-amylase was found sensitive to TP treatment. Tea polyphenols exhibited IC50 at 0.41 mg mL−1 against PPA and maximum inhibitory rate (98.17%) at 3.0 mg mL−1. Tea polyphenols inhibition was concluded as noncompetitive pattern based on its unchanged Km value (0.98 mg mL−1) for soluble starch substrate. Tea polyphenols inhibition arose from pH 1.5 to 10.14, covering gastric and intestinal environments inside body. Circular dichroism spectra analysis revealed regular changes of PPA in secondary conformations (increased proportions of α-helix and β-sheet) prior to its inactivation at low TP concentrations. Tea polyphenols-inhibited PPA had distinct double-negative peaks at 204 nm and 208 nm. Porcine pancreas α-amylase was inactivated by TP in ways of complexation and modification of secondary conformations. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
09505423
Volume :
51
Issue :
6
Database :
Academic Search Index
Journal :
International Journal of Food Science & Technology
Publication Type :
Academic Journal
Accession number :
115403973
Full Text :
https://doi.org/10.1111/ijfs.13120