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Quercetin (Que) is a flavonoid widely distributed in vegetables and fruits and exhibits strong antioxidant activity,but the poor stability of Que limits its function and application.The present study developed a nanoparticle (NP) using bovine serum albumin (BSA) as a matrix to encapsulate Que.The stability of encapsulated Que by BSA NP was tracked in a simulated intestinal fluid (SIF).The antioxidant activity of encapsulated Que was evaluated by the 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,20azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging assays.Furthermore,the stabilizing mechanism of Que by BSA NP was investigated,using scanning transmisson electron microscopy (STEM),dynamic light scattering (DLS),UVvis,fluorescence spectrometry,and circular dichroism (CD).The results revealed that Que was effectively encapsulated by BSA and formed spherical NP (<10 nm).BSA NP not only promoted the stability of encapsulated Que but also kept the antioxidant activity of encapsulated Que.The driving forces for BSAQue association were hydrophobic interaction and hydrogen bond,and the latter was involved in the mechanism of Que stabilization.This suggested that BSA NP could be a good carrier to deliver hydrophobic flavonols.