Dipeptidyl Peptidase-4 Inhibitory Activity of Casein Glycomacropeptide Hydrolysates(酪蛋白糖巨肽酶解物的二肽基肽酶-4抑制作用)
摘要
The aim of the present study was to investigate the dipeptidyl peptidase-4 (DPP-4) inhibitory activity of glycomacropeptide (GMP) hydrolysates obtained with papain, alkaline, trypsin and protease. The DPP-4 activity was assayed by the chromogenic substrate with Gly-Pro-PNA as a substrate in vivo. GMP hydrolysates showed a higher DPP-4 inhibitory rate than native GMP. The DPP-4 inhibitory activity of GMP hydrolysates increased during the hydrolysisperiods. GMP hydrolysates obtained by papain possessed the greatest DPP-4 inhibitory activity. The papain-treated GMP may have the potential application as DPP-4 inhibitor.(为探讨酪蛋白糖巨肽(GMP)酶解物的二肽基肽酶-4(DPP-4)抑制作用,选择木瓜蛋白酶、碱性蛋白酶、胰蛋白酶、胃蛋白酶分别酶解GMP获得糖巨肽酶解物,选择甘氨酰脯氨酸对硝基苯胺为底物的发色底物法检测DPP-4活性。结果表明,GMP酶解物的DPP-4抑制效果优于GMP本身,并且随酶解时间的延长酶解物DPP-4抑制作用逐渐增加,其中GMP木瓜蛋白酶解物对DPP-4抑制效果最好,GMP木瓜蛋白酶酶解物作为DPP-4抑制剂具有潜在应用价值。)