Multispectral and molecular docking methods were used to study the interaction mode and mechanism of two important components of whey proteins, lactoferrin (LF) and β-lactoglobulin (β-LG), and of a lactone sophorolipid (LSL) mixed system. The preservation effect of the mixed system on milk was also studied and compared. The results showed that the quenching mechanism of LSL on both β-LG and LF was static, but that the non-covalent complexes formed were the result of the different interacting forces: hydrogen bonds and the van der Waals force for the LSL-β-LG system, and electrostatic force for the LSL-LF system. The binding constants of LSL-β-LG and LSL-LF were all relatively small, and the interaction of LSL with β-LG was stronger than its interaction with LF. After adding β-LG, LF, or the mixed system with LSL to the milk, the stability of milk emulsion was effectively improved in all cases, while the preservative ability was effectively enhanced only by the addition of LF or LSL-LF. These results provide supportive data and a theoretical basis for enhancing the production of dairy products and other byproducts.
Keywords: interaction mechanism; lactoferrin (LF); lactone sophorolipid (LSL); preservative effect; β-lactoglobulin (β-LG).