Inhibitory effect and mechanism of cinnamic acid on α-amylase

  • LYU Junli ,
  • YUN Yueying ,
  • REN Yan ,
  • HE Xuan
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  • (School of Life Science & Technology, Inner Mongolia University of Science & Technology, Baotou 014010, China)

Received date: 2025-04-11

  Revised date: 2025-05-16

  Online published: 2026-01-22

Abstract

This study aimed to elucidate the inhibitory properties of cinnamic acid on α-amylase by investigating its inhibitory effects and underlying mechanisms through a combination of spectroscopic techniques and molecular docking methods.The findings indicated that cinnamic acid exhibited the highest inhibition rate of α-amylase, reaching 78.05%, within the concentration range of 0.04 to 0.20 mmol/L.Ultraviolet (UV) spectral analysis demonstrated that the characteristic peak position of α-amylase remained unchanged with increasing concentrations of cinnamic acid, although the absorption of UV light by α-amylase at a constant wavelength increased in a concentration-dependent manner.Fluorescence spectroscopy revealed the existence of a binding site between cinnamic acid and α-amylase, with the quenching mechanism identified as static quenching.The interaction between cinnamic acid and α-amylase was characterized by an enthalpy change (ΔH) of 134.785 kJ/mol and an entropy change (ΔS) of 504.552 J/(mol·K), both of which were positive, suggesting that hydrophobic interactions were the predominant forces involved.Molecular docking analyses revealed that the minimum binding energy between cinnamic acid and α-amylase was -23.263 kJ/mol.In addition to hydrophobic interactions, van der Waals forces and hydrogen bonding were identified as significant contributors to the stability of the cinnamic acid and α-amylase complex.These findings suggest that cinnamic acid possesses potential inhibitory effects on α-amylase activity, thereby providing a theoretical basis for the development of functional foods aimed at managing type 2 diabetes.

Cite this article

LYU Junli , YUN Yueying , REN Yan , HE Xuan . Inhibitory effect and mechanism of cinnamic acid on α-amylase[J]. Food and Fermentation Industries, 2026 , 52(1) : 237 -243 . DOI: 10.13995/j.cnki.11-1802/ts.042989

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