Soy protein was hydrolyzed using two enzymes to obtain soy protein hydrolysate (SPH), the SPH was fractionated with ultrafiltration membranes to obtain peptide fractions below 1,000 Da (SP1) and 1,000-5,000 Da (SP2), and for the meantime, SPH was further completely hydrolyzed to get compound amino acids (CAA). Maillard reaction products (MRPs) were prepared from aqueous xylose-SPH/SP1/SP2/CAA model systems by heating at 120A degrees C for 2.0 h. Compared with the original hydrolysates and other MRPs, the MRPs from SP2 exhibited a distinctly enhanced effect on flavor, including the caramel-like, soy sauce-like odors, umami and mouthful tastes and a greatly reduced bitterness in consommeA ' soup. Antioxidant activities of SPH, SP1, SP2, CAA, and their MRPs were investigated through reducing power, DPPH radical-scavenging activity, and Fe2+ chelating activity. Before Maillard reaction, the antioxidant activities of peptide fractions with different molecular weights were quite different, and SP2 showed the highest activity; however, CAA exhibited very poor antioxidant activity. The antioxidant activities of SPH, SP1, SP2, and CAA were greatly enhanced by Maillard reaction, and the MRPs prepared from xylose-CAA model system exhibited a higher antioxidant activity than those from other model systems. Pyrazines, pyrroles, furans, and thiazoles were significantly correlated with reducing power and Fe2+ chelating activity by principal component analysis.