RESUMEN
As the largest emitter of greenhouse gases, the livestock and poultry industry is facing the challenge of increasing production to meet global demand while reducing environmental impacts. Improving feed digestibility by optimizing feed structure (e.g., exogenous additive) is one of the green breeding measures to alleviate carbon pressure. In this study, the interaction mechanism and in vitro digestibility properties of puerarin (PUE) with feed proteins (zein and soy protein isolate (SPI)) to form Zein-PUE and SPI-PUE complexes were investigated mainly by multispectral and molecular docking techniques. Results indicated that the addition of PUE improved the physicochemical properties of proteins (e.g., solubility and disulfide bond contents). Then, the spectral results showed that the binding processes were spontaneous, and the protein structure tended to loose and disordered after binding, and more hydrophobic residues were exposed to the hydrophilic microenvironment. Moreover, on the basis of molecular docking revealed that PUE bound to zein by hydrogen bond, electrostatic and hydrophobic interactions, while with SPI by hydrogen bond and hydrophobic interaction. Finally, in vitro digestion experiments demonstrated that the bioavailability of Zein-PUE and SPI-PUE complexes increased by 1.15 % and 2.11 %, respectively. Overall, PUE is a promising feed additive beneficial for enhancing protein digestibility and bioavailability.