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 2,2'-azinobis(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), UV-vis, 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 BSA-Que 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.

Amino acids have attracted increasing attention in developing effective inhibitors on acrylamide (AA) formation during food processing. The main purpose of this study was to evaluate the inhibitory effect and mechanism of taurine (Tau) on AA formation. In the presence of Tau, AA formation was effectively inhibited in asparagine ⁄ glucose (Asn ⁄ Glc) model system. Results also showed that Glc content was decreased as Glc-Tau solution was heated, which indicated that Tau could react directly with Glc in the Maillard reaction. LC-QTOF MS revealed two peaks in extracted ion chromatograms [M + H] + at m ⁄ z 197 and m ⁄ z 268 during the thermal treatment, which were identified as AA-Tau and AA dimmer-Tau adducts, respectively. Our results demonstrated that inhibitory effect of Tau on AA formation was not only mediated through contesting consumption of Glc with Asn, but also directly reacting with AA to promote formation of AA-Tau and AA dimer-Tau adducts.