کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5137180 | 1494534 | 2017 | 12 صفحه PDF | دانلود رایگان |

- Qula casein was hydrolyzed by different enzymes for the production of ACEI peptides.
- Hydrolysates with the highest ACEI activities were selected for LC-MS/MS analysis.
- Four QSAR models were established to predict potential ACEI peptides.
- Molecular docking studies explored potential ACEI activities of selected peptides.
- PFPGPIPN, KYIPIQ and LPLPLL were chemically prepared to determine ACEI activities.
Qula casein derived from yak milk was hydrolysed using various enzymes. Hydrolysates were withdrawn at different hydrolysis phases and were determined to their degree of hydrolysis (DH) and ACE (angiotensin I-converting enzyme) inhibitory (ACEI) activities. Using a 3Â kDa ultra-filtration membrane, hydrolysates were fractioned into two ranges of molecular weight and permeated fractions were further investigated. A Lineweaver-Burk plot was used to explore the ACEI kinetics of the hydrolysates. Additionally, the peptides in the hydrolysates were identified using LC-MS/MS. We established four quantitative structure-activity relationship (QSAR) models for predicting potential ACEI peptides. Using in silico analysis, four novel ACEI peptides were identified and a molecular docking study further explored the potential ACEI activities. Based on the docking results, three new peptides (PFPGPIPN, KYIPIQ and LPLPLL) were chemically synthesized and their IC50 values were determined. In conclusion, our study suggests that Qula casein may be a valuable source of ACEI peptides.
Journal: Journal of Functional Foods - Volume 32, May 2017, Pages 266-277