Inhibition mechanism of ferulic acid against α-amylase and α-glucosidase

Yuxue Zheng; Jinhu Tian; Wenhan Yang; Shiguo Chen; Donghong Liu; Haitian Fang; Huiling Zhang; Xingqian Ye

doi:10.1016/j.foodchem.2020.126346

Inhibition mechanism of ferulic acid against α-amylase and α-glucosidase

Food Chem. 2020 Jul 1:317:126346. doi: 10.1016/j.foodchem.2020.126346. Epub 2020 Feb 3.

Authors

Yuxue Zheng¹, Jinhu Tian², Wenhan Yang¹, Shiguo Chen¹, Donghong Liu³, Haitian Fang⁴, Huiling Zhang⁴, Xingqian Ye⁵

Affiliations

¹ Zhejiang University, Department of Food Science and Nutrition, Zhejiang Key Laboratory for Agri-Food Processing, Fuli Institute of Food Science, Zhejiang R&D Centre for Food Technology and Equipment, Hangzhou 310058, China.
² Zhejiang University, Department of Food Science and Nutrition, Zhejiang Key Laboratory for Agri-Food Processing, Fuli Institute of Food Science, Zhejiang R&D Centre for Food Technology and Equipment, Hangzhou 310058, China. Electronic address: jinhutian@126.com.
³ Zhejiang University, Department of Food Science and Nutrition, Zhejiang Key Laboratory for Agri-Food Processing, Fuli Institute of Food Science, Zhejiang R&D Centre for Food Technology and Equipment, Hangzhou 310058, China; Ningbo Research Institute, Zhejiang University, Ningbo 315100, China.
⁴ Ningxia University, Ningxia Key Laboratory for Food Microbial-Applications Technology and Safety Control, Yinchuan 750021, China.
⁵ Zhejiang University, Department of Food Science and Nutrition, Zhejiang Key Laboratory for Agri-Food Processing, Fuli Institute of Food Science, Zhejiang R&D Centre for Food Technology and Equipment, Hangzhou 310058, China. Electronic address: psu@zju.edu.cn.

PMID: 32070843
DOI: 10.1016/j.foodchem.2020.126346

Abstract

The inhibitory mechanisms of ferulic acid against α-amylase and α-glucosidase were investigated by enzyme kinetic analysis, circular dichroism (CD), Fourier-transform infrared (FT-IR) spectroscopy, fluorescence quenching and molecular docking. Results indicated that ferulic acid strongly inhibited α-amylase (IC₅₀: 0.622 mg ml^-1) and α-glucosidase (IC₅₀: 0.866 mg ml^-1) by mixed and non-competitive mechanisms, respectively. CD spectra and fluorescence intensity measurements confirmed that the secondary structure of α-amylase and α-glucosidase were changed and the microenvironments of certain amino acid residues were modulated by the binding of ferulic acid. FT-IR spectra indicated that the interaction between ferulic acid and α-amylase/α-glucosidase mainly involved in non-covalent bonds. Molecular docking further demonstrated that the interaction forces between ferulic acid and α-amylase/α-glucosidase were hydrogen bonds, with the binding energy of -5.30 to -5.10 and -5.70 kcal mol^-1, respectively. This study might provide a theoretical basis for the designing of novel functional foods with ferulic acid.

Keywords: Digestive enzymes; Ferulic acid; Inhibition; Molecular docking; Starch digestion.

MeSH terms

Binding Sites
Coumaric Acids / chemistry
Coumaric Acids / metabolism*
Glycoside Hydrolase Inhibitors / chemistry
Glycoside Hydrolase Inhibitors / metabolism*
Hydrogen Bonding
Kinetics
Molecular Docking Simulation
Protein Structure, Secondary
Thermodynamics
alpha-Amylases / chemistry
alpha-Amylases / metabolism*
alpha-Glucosidases / chemistry
alpha-Glucosidases / metabolism*

Substances

Coumaric Acids
Glycoside Hydrolase Inhibitors
ferulic acid
alpha-Amylases
alpha-Glucosidases