Revealing the interaction modes between nanoscale metal-organic frameworks (NMOFs) and food matrix is crucial for functional release but it still remains largely unknown to date. This study specifically focused on the milk protein adsorption mechanism of NMOFs using UiO66/UiO66-NH2 and β-lactoglobulin (β-LG) as models. UiO66 and UiO66-NH2 quenched the fluorescence of β-LG via static mechanism. Due to the enhanced electrostatic forces caused by NH2, UiO66-NH2-β-LG (2.83 × 105 mol·L-1) exhibited higher binding constant than UiO66-β-LG (2.61 × 105 mol·L-1), while UiO66 with higher hydrophobicity adsorbed more β-LG. The defects of UiO influenced the binding sites on the β-LG, and the higher the defect degree, the higher the binding energy. For the stability of the system, the H-bonding between UiO66 and SER30/PRO38, and the hydrophobic interaction between UiO66-NH2 and LYS101 played important roles. Furthermore, the secondary structure content of β-LG changed after interacting with both UiO, resulting in reduced density of β-LG.
Keywords: Bridging linker; Interaction; Metal-organic frameworks; β-Lactoglobulin.
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