Screening and Characterization of an α-Amylase Inhibitor from Carya cathayensis Sarg. Peel
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Updated: Jul 7, 2025

Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System
Published on: August 8, 2016
Xiaosan Zhang1, Guangrong Huang1, Hua Liu2
1Key Laboratory of Specialty Agri-Product Quality and Hazard Controlling Technology of Zhejiang Province, College of Life Sciences, China Jiliang University, Hangzhou 310018, China.
Abstract:
Inhibiting α-amylase can lower postprandial blood glucose levels and delay glucose absorption, offering an effective approach for the development of antidiabetic diets. In this study, an active constituent with inhibitory activity against α-amylase was isolated and purified by bioassay-guided fractionation from Carya cathayensis Sarg. peel (CCSP). The active constituent was identified by NMR and Q-Exactive Orbitrap Mass Spectrometry as 5-O-p-coumaroylquinic acid (5-CQA). 5-CQA possessed strong inhibitory activity against α-amylase, with an IC50 value of 69.39 µM. In addition, the results of the kinetic study indicated that 5-CQA was a potent, reversible, noncompetitive inhibitor against α-amylase. The findings indicate that 5-CQA derived from CCSP has potential as a novel inhibitor against α-amylase, which can help mitigate postprandial blood sugar spikes, making it suitable for inclusion in antidiabetic diets.
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