酪蛋白ACE抑制肽的分离纯化

Object: For separation and purification of casein hydrolysate to obtain the novel amino acid sequences of ACE inhibitory peptides with high-activity and small molecular weight. Method: On the basis of the ACE inhibitory peptides from casein hydrolysed by Alcalase 2.4L and Neutrase 1.5MG proteases, the casein hydrolysate were purified by macroporous adsorption resin, sephadex G-15 gel filtration column, preparative and analytic RP-HPLC. The amino acid sequences of ACE inhibitory peptides were identified by LC-ESI/MS/MS. Results: Four casein ACE inhibitory peptides were obtained with amino acid sequences LY, WKQ, WQV and LQSW, the IC50 of ACE inhibiting activity were 23.8 μg/mL, 48.5 μg/mL, 40.8 μg/mL and 28.0 μg/mL, respectively. Conclusion: The results indicated that these four peptides all have smaller molecular weight and higher ACE inhibitory activities. ACE inhibitory peptides WKQ, WQV and LQSW are reported for the first time.