Effect and mechanism of chlorogenic acid inhibition of starch enzymatic hydrolysis: Comparison of different processing methods

The inhibitory mechanism of chlorogenic acid (CA) on starch enzymolysis was explored in terms of the effects of on amylases and starch. Molecular docking, circular dichroism and fluorescence spectroscopy were used to study the interaction between CA and amylases. CA changed the secondary structure of amylases, caused fluorescence quenching, and linked to α-amylase and amylglucosidase with binding energy of −12.7 and − 2.1 kcal/mol through hydrogen bonds, electrostatic interactions, and hydrophobic interactions. The rapidly digested starch (RDS) content of the CA-potato/corn starch complexes decreased to 34.72 % and 28.09 %. Enzyme kinetics, degradation kinetics and thermodynamics results indicated the enzymolysis of complexes had lower maximum reaction rate ( V m ), higher Michaelis-Menten constant ( K m ), activation energy ( E a ) and enthalpy variation (Δ H ), reflecting a lower affinity between complexes and amylases . Furthermore, the complexes showed more compact structure. This study helps regulate starch digestion, showing a positive effect on balancing blood glucose level and controlling chronic diseases. • Investigate the interaction between chlorogenic acid and two amylases. • Study the mechanism of chlorogenic acid acting on starch enzymolysis inhibition. • The effect of CA on amylase hydrolysis in complex was studied.