Purification and Identification of a Novel Angiotensin I-Converting Enzyme Inhibitory Peptide from Sesame Meal
作者： Wenping Liu , Guangyan Cheng , Huimin Liu , Yi Kong
DOI: 10.1007/S10989-015-9471-Y
关键词:
摘要: An angiotensin I-converting enzyme (ACE) inhibitory peptide was isolated and identified from sesame meal by successive chromatography. Sesame hydrolysates were obtained treatment with alcalase, papain, neutrase pepsin. The ACE activities of each hydrolysate investigated the alcalase produced highest activity. protein generated then separated an ultrafiltration membrane 10 kDa molecular weight cut-off membranes, Sephadex G-50 semi preparative reversed-phase high-performance liquid chromatography (RP-HPLC). Biological functions all fractions assayed, Y4, a fraction RP-HPLC, found to display Y4 873.3 Da amino acid sequence Tyr-Ala-His-Tyr-Ser-Tyr-Ala determined TOF–MS/MS. IC50 value for activity 0.6 mg/mL. These results suggested that may be beneficial ingredient nutraceuticals pharmaceuticals against hypertension its related diseases.
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