2. Academic Validation
  3. Screening and Characterization of an α-Amylase Inhibitor from Carya cathayensis Sarg. Peel

Screening and Characterization of an α-Amylase Inhibitor from Carya cathayensis Sarg. Peel

  • Foods. 2023 Dec 10;12(24):4425. doi: 10.3390/foods12244425.
Xiaosan Zhang 1,  Guangrong Huang 1,  Hua Liu 2,  Wenwei Chen 1,  Jing Zhao 1,  Zhenbao Jia 1,  Fei Tao 3
Affiliations

Affiliations

  • 1 Key Laboratory of Specialty Agri-Product Quality and Hazard Controlling Technology of Zhejiang Province, College of Life Sciences, China Jiliang University, Hangzhou 310018, China.
  • 2 Food and Drug Inspection and Testing Center of Chunan County, Hangzhou 310022, China.
  • 3 College of Standardization, China Jiliang University, Hangzhou 310018, China.
PMID: 38137229 DOI: 10.3390/foods12244425
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.

Keywords

5-O-p-coumaroylquinic acid; Carya cathayensis Sarg. Peel; postprandial hyperglycemia; α-amylase inhibitor.

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