Li Jiaxin, Yang Danyin, Xu Qiongyao, Huang Mingtao, Zheng Lin, Zhao Mouming
School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China.
School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China.
Food Chem. 2025 Oct 15;489:144970. doi: 10.1016/j.foodchem.2025.144970. Epub 2025 May 28.
Gly-Pro-type peptides consisting of 4-9 amino acids are the most potent DPP-IV inhibitory peptides in collagen. In this study, we investigated the release patterns of collagen-derived Gly-Pro-type peptides with DPP-IV inhibitory activities by analyzing the cleavage selectivity of proteases, and the dynamic release mechanism of Gly-Pro-type peptides. Results showed that collagen hydrolysate with the highest DPP-IV inhibitory activity was obtained by proteaC (IC = 0.58 ± 0.02 mg/mL). Large amounts of Gly-Pro-type peptides consisting of 4, 6, and 9 amino acids were released. ProteaC preferred to cleave Gly and hydrophobic amino acids residues at the P1' position, and had a strong cleavage preference for Hyp residue at the P1 position. The dynamic release mode indicated that the release of potent DPP-IV inhibitory peptides underwent a change from precursor peptides to target peptides and then to short peptides. These findings provided a better understanding of the release of DPP-IV inhibitory peptides.
由4至9个氨基酸组成的甘氨酰-脯氨酸型肽是胶原蛋白中最有效的二肽基肽酶-IV（DPP-IV）抑制肽。在本研究中，我们通过分析蛋白酶的切割选择性以及甘氨酰-脯氨酸型肽的动态释放机制，研究了具有DPP-IV抑制活性的胶原蛋白衍生甘氨酰-脯氨酸型肽的释放模式。结果表明，通过蛋白酶C（IC = 0.58±0.02 mg/mL）可获得具有最高DPP-IV抑制活性的胶原蛋白水解产物。释放出了大量由4、6和9个氨基酸组成的甘氨酰-脯氨酸型肽。蛋白酶C倾向于在P1'位置切割甘氨酸和疏水性氨基酸残基，并且对P1位置的羟脯氨酸残基有很强的切割偏好。动态释放模式表明，强效DPP-IV抑制肽的释放经历了从前体肽到目标肽再到短肽的变化。这些发现有助于更好地理解DPP-IV抑制肽的释放。
