The inhibitory mechanism of chlorogenic acid and its acylated derivatives on α-amylase and α-glucosidase

Shan Wang; Yue Li; Dejian Huang; Shangwei Chen; Yongmei Xia; Song Zhu

doi:10.1016/j.foodchem.2021.131334

The inhibitory mechanism of chlorogenic acid and its acylated derivatives on α-amylase and α-glucosidase

Food Chem. 2022 Mar 15:372:131334. doi: 10.1016/j.foodchem.2021.131334. Epub 2021 Oct 5.

Authors

Shan Wang¹, Yue Li², Dejian Huang³, Shangwei Chen⁴, Yongmei Xia⁴, Song Zhu⁵

Affiliations

¹ State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; International Joint Laboratory on Food Safety, Jiangnan University, Wuxi, Jiangsu 214122, China.
² State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
³ Department of Food Science and Technology, National University of Singapore, Singapore 117543, Singapore.
⁴ State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
⁵ State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; International Joint Laboratory on Food Safety, Jiangnan University, Wuxi, Jiangsu 214122, China. Electronic address: zhusong@jiangnan.edu.cn.

PMID: 34638063
DOI: 10.1016/j.foodchem.2021.131334

Abstract

Due to the poor lipophilicity of chlorogenic acid (CA), five CA derivatives (C2-CA, C4-CA, C6-CA, C8-CA, and C12-CA) with different lipophilicities were synthesized using acylation catalyzed by lipase in present study. The inhibitory activities and mechanisms of CA and its derivatives on α-amylase and α-glucosidase were then determined. Results showed that the inhibitory activities of CA derivatives on α-amylase and α-glucosidase were enhanced as lipophilicity increased, and the inhibitory activities of C12-CA were stronger than those of CA. IC₅₀ values of C12-CA were 13.30 ± 0.26 μmol/mL for α-amylase and 3.42 ± 0.10 μmol/mL for α-glucosidase. C12-CA possessed the smallest K_ic and K_iu values, and its inhibitory actions on α-amylase and α-glucosidase were stronger than those of CA and the other derivatives. Effects of C12-CA on microenvironments of amino acid residues and secondary structures of α-amylase and α-glucosidase were greater than those of CA and the other derivatives.

Keywords: Chlorogenic acid derivatives; Fluorescence quenching; Inhibitory kinetics; α-Amylase; α-Glucosidase.

MeSH terms

Chlorogenic Acid
Glycoside Hydrolase Inhibitors
Lipase
alpha-Amylases*
alpha-Glucosidases*

Substances

Glycoside Hydrolase Inhibitors
Chlorogenic Acid
Lipase
alpha-Amylases
alpha-Glucosidases