Hemp seed protein and chlorogenic acid complex: Effect of ultrasound modification on its structure and functional properties

In this study, the effects of ultrasound and chlorogenic acid (CA) on the structural and functional properties of hemp seed protein (HSP) was investigated. Compared with natural HSP, the UV-vis spectra intensity of ultrasound-treated HSP (UHSP) and UHSP-CA increased, the fluorescence spectra intensity decreased with a red shift in the maximum intensity peak. The results showed that ultrasound modification and complexation with CA unfolded the structure of HSP exposing its internal groups. Fluorescence quenching analysis showed that the best binding between UHSP and CA (binding constant 2.94 x 102 L/mol) was achieved at 450 W for 15 min of ul-trasound treatment. In addition, the same ultrasound conditions minimized the particle size and surface roughness of UHSP and UHSP-CA. The solubility of UHSP and UHSP-CA increased by 23.3 and 38.7 %, the emulsifying activity index increased by 16.9 and 16.2 %, and the emulsion stability index increased by 20.9 and 20.8 %, respectively. These results indicated that appropriate ultrasound treatment and complexation with CA can significantly modify the structural and functional properties of HSP, improving its application value in the food field.

Automated summary

This study investigated the effects of ultrasound and chlorogenic acid (CA) on the structural and functional properties of hemp seed protein (HSP). The results showed that ultrasound treatment and complexation with CA unfold the structure of HSP, exposing its internal groups. The best binding between ultrasound-treated HSP and CA was achieved at 450 W for 15 min of ultrasound treatment. Additionally, the same ultrasound conditions minimized the particle size and surface roughness of the proteins, and improved their solubility and emulsifying properties.