Abstract Title:

A new functionality study of vanillin as the inhibitor forα-glucosidase and its inhibition kinetic mechanism.

Abstract Source:

Food Chem. 2021 Mar 3 ;353:129448. Epub 2021 Mar 3. PMID: 33711702

Abstract Author(s):

Yujia Liu, Jie Zhu, Jiamei Yu, Xu Chen, Shuyan Zhang, Yanxue Cai, Lin Li

Article Affiliation:

Yujia Liu


Vanillin is a natural phenolic compound mainly used as flavors in food industry. In this work, a new functionality of vanillin as theα-glucosidase inhibitor was studied based on the inhibition kinetic mechanism. The inhibitory effect (IC50) of vanillin against α-glucosidase was 28.34 ± 0.89 mg/mL, which belongs to mixed inhibition mechanism and its process was spontaneous. Vanillin could bind to α-glucosidase by hydrophobic interactions and hydrogen bonds with -8.42 kcal/mol intermolecular energy to form the steric hindrance. The average binding distances was calculated as 2.20 nm according to energy transfer theory. In addition, the protein secondary structure and denaturation temperature (decreasing about 10 °C) were changed significantly after vanillin binding to α-glucosidase, resulting in an inhibitory effect. The findings of this research provide insights for the development of vanillin as potential inhibitor for α-glucosidase in special dietary foods.

Study Type : In Vitro Study

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Sayer Ji
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