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Maltoheptaoside hydrolysis with chromatographic detection and starch hydrolysis with reducing sugar analysis: Comparison of assays allows assessment of the roles of direct α-amylase inhibition and starch complexation
- Source :
- Food chemistry. 343
- Publication Year :
- 2020
-
Abstract
- The aim was to determine inhibition of human α-amylase activity by (poly)phenols using maltoheptaoside as substrate with direct chromatographic product quantification, compared to hydrolysis of amylose and amylopectin estimated using 3,5-dinitrosalicylic acid. Acarbose exhibited similar IC50 values (50% inhibition) with maltoheptaoside, amylopectin or amylose as substrates (2.37 ± 0.11, 3.71 ± 0.12 and 2.08 ± 0.01 µM respectively). Epigallocatechin gallate, quercetagetin and punicalagin were weaker inhibitors of hydrolysis of maltoheptaoside ( epigallocatechin gallate > quercetagetin, with minimal interference using maltoheptaoside as substrate. The main inhibition mechanism of epigallocatechin gallate and punicalagin was through complexation with starch, especially amylose, whereas only quercetagetin additionally binds to the α-amylase active site. Interference is minimised using maltoheptaoside as substrate with product detection by chromatography, potentially allowing assessment of direct enzyme inhibition by almost any compound.
- Subjects :
- Starch
Quercetagetin
Amylopectin
Oligosaccharides
Epigallocatechin gallate
01 natural sciences
Catechin
Analytical Chemistry
chemistry.chemical_compound
Hydrolysis
0404 agricultural biotechnology
Amylose
Catalytic Domain
Humans
Amylase
Chromatography
biology
Chemistry
010401 analytical chemistry
food and beverages
Substrate (chemistry)
Polyphenols
04 agricultural and veterinary sciences
General Medicine
Chromatography, Ion Exchange
Flavones
040401 food science
Hydrolyzable Tannins
Salicylates
0104 chemical sciences
biology.protein
Acarbose
alpha-Amylases
Sugars
Food Science
Subjects
Details
- ISSN :
- 18737072
- Volume :
- 343
- Database :
- OpenAIRE
- Journal :
- Food chemistry
- Accession number :
- edsair.doi.dedup.....6ae68590e9e17bd8f84e4867bb94aa18