Bone collagen hydrolysates (peptides) derived from byproduct of animal product processing have been used to produce commercially valuable products due to their potential antioxidant activity. Maillard glycosylated reaction is considered as a promising method to enhance the antioxidant activity of peptides. Hence, this research aims at investigating the Maillard glycosylation activity and antioxidant activity of bone collagen hydrolysates from different sources. In this study, 3 glycosylated bone collagen hydrolysates were prepared and characterized, and cytotoxicity and antioxidant activity were analyzed and evaluated. The free amino groups loss, browning intensity, and fluorescence intensity of G-Cbcp (glycosylated chicken bone collagen hydrolysates (peptides)) were the heaviest, followed by G-Pbcp (glycosylated porcine bone collagen hydrolysates (peptides)) and G-Bbcp (glycosylated bovine bone collagen hydrolysates (peptides)). The results of amino acid analysis showed that amino acid composition of different bone collagen hydrolysates was significantly different and the amino acid decreased to different degrees after Maillard glycosylated reaction, which may lead to differences in Maillard glycosylated reaction activity. Furthermore, the 3 glycosylated hydrolysates showed no significant cytotoxicity. The results showed that glycosylation process significantly increased the antioxidant activity of bone collagen hydrolysates, and G-Cbcp showed the strongest antioxidant activity, followed by G-Pbcp and G-Bbcp. Therefore, compared with the bone collagen hydrolysates, 3 glycosylated hydrolysates showed significant characteristic and structural changes, and higher antioxidant activity.