Insighting the effect of ultrasound-assisted polyphenol non-covalent binding on the functional properties of myofibrillar proteins from golden threadfin (Nemipterus virgatus)

Abstract

In this study, the effect of ultrasound-assisted non-covalent binding of different polyphenols (tannins, quercetin, and resveratrol) on the structure and functional properties of myofibrillar proteins (MP) from the golden threadfin (Nemipterus virgatus) was investigated. The effect of ultrasound-assisted polyphenol incorporation on the structure and properties of MP was evaluated by multispectral analysis, interfacial properties, emulsification properties and antioxidant properties et al. The results revealed that the protein–polyphenol interaction led to a conformational change in the microenvironment around the hydrophobic amino acid residues, resulting in an increase in the equilibrium of the MP molecules in terms of affinity and hydrophobicity. Ultrasound assisted polyphenols addition also led to a significant decrease of the oil/water interfacial tension (from 21.22 mN/m of MP to 8.66 mN/m of UMP-TA sample) and a significant increase of the EAI (from 21.57 m²/g of MP to 28.79 m²/g of UMP-TA sample) and ES (from 84.76 min of MP to 124.25 min of UMP-TA). In addition, ultrasound-assisted polyphenol incorporation could enhance the antioxidant properties of MP, with the DPPH and ABTS radical scavenging rate of UMP-TA increase of 47.7 % and 55.2 % in comparison with MP, respectively. The results demonstrated that the noncovalent combination with polyphenols under ultrasound-assisted conditions endowed MP with better functional properties, including solubility, emulsification, foaming, and antioxidant properties through structure change. This study can provide innovative theoretical guidance for effectively preparing aquatic protein–polyphenol non-covalent complexes with multiple functions and improving the processing and utilization value of aquatic proteins.