Interaction and binding mechanism of ovalbumin with cereal phenolic acids: improved structure, antioxidant activity, emulsifying and digestion properties for potential targeted delivery systems.

Ovalbumin (OVA) has been considered as a nutrient carrier for bioactive, which has high nutrition value and multiple properties. Recently, proteins-phenolic acids composite delivery systems have received widespread attention. Therefore, this research aimed to investigate the interaction between OVA and cereal phenolic acids (CPA) to establish delivery systems for bioactive. Spectroscopy results have found that CPA generated complexes with OVA, causing the microenvironment changes of OVA. Ferulic acid (FA), p-coumaric acid (CA), vanillic acid (VA), syringic acid (SY), sinapic acid (SI), and protocatechuic acid (PA) not only quenched the intrinsic fluorescence of OVA, but also altered protein microenvironment. Further investigation showed these complexes were formed by static quenching mode, while hydrogen bond and hydrophobic interaction were dominant binding forces. Meanwhile, the interaction decreased α-helix contents and increased β-sheet contents, leading to conformational changes in OVA. Besides, OVA/CPA complexes displayed an increase in hydrophobicity with a reduce in free-SH. After combination with FA, SY, CA, VA, SI, PA, it was found that all formed complexes had superior solubility, emulsifying and antioxidant activities than native OVA. Among them, OVA-PA exhibited the highest emulsifying activity index and emulsion stability index values (36.4 ± 0.39 m

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Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.