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BACKGROUND Dual modification of collagen was performed using ionic liquid (IL) and ultrasound (US) to modulate the activity of collagen hydrolyzed peptides and reveal the production mechanism of cowhide-derived DPP-IV inhibitory peptides. RESULTS The results revealed that dual modification (IL+US) significantly improved the hydrolytic degree (DH) of collagen (P < 0.05). Meanwhile, ionic liquid and ultrasound tended to promote the break of hydrogen bonds, whereas inhibit the crosslinking between collagens. The double modification reduced the thermal stability and accelerated the exposure of tyrosine and phenylalanine of collagen, and improved the proportion of small molecular (< 1 KDa) peptides in collagen hydrolysates. Interestingly, the hydrophobic amino acid (HAA) residues and DPP-IV inhibitory activity of collagen peptides with small molecular weight (< 1 KDa) was increased further under the combination of IL and ultrasound. CONCLUSION Hence, enhanced hypoglycemic activity of collagen peptides can be attained through the dual modification of ionic liquid and ultrasound. This article is protected by copyright. All rights reserved.