The effects of two glycosylated whey hydrolysates (GWH-Gal A and GWH-Gal B) on glutathione (GSH) and related antioxidant enzymes in SGC-7901 cells were evaluated. Two whey glycosylated hydrolysates promoted an increase in reduced glutathione (GSH) in normal SGC-7901 cells. GSH, glutathione peroxidase (GPx), gamma glutamine cysteine synthetaase (gamma-GCS), and catalase (CAT) at 1.0 and 2.0 mg/mL in normal SGC-7901 cells were higher in the GWH-Gal A group than in the GWH-Gal B group (P < 0.05). Compared with GWH-Gal B, GWH-Gal A more strongly inhibited decreases in intracellular GSH, GPx, gamma-GCS, CAT, and superoxide dismutase (SOD) in H2O2-induced SGC-7901 cells. Compared with GWH-Gal B, GWH-Gal A at 1.0 and 2.0 mg/mL effectively inhibited increases in lactate dehydrogenase (LDH) and malondialdehyde (MDA) in H2O2-induced SGC7901 cells (P < 0.05). Therefore, GSH content and related antioxidant enzyme activity levels (GPx, gamma-GCS, CAT, SOD) in both normal and H2O2-induced SGC-7901 cells were considerably stronger in the GWH-Gal A group than in the GWH-Gal B group.