Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 65, Issue 42, Pages 9324-9332Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.7b03203
Keywords
lactic acid bacteria; enzyme specificity; bioactive peptides; tandem mass spectrometry; sheep milk; casein hydrolysate; QSAR
Funding
- Spanish Ministry of Economy and Competitiveness (MINECO) [AGL2015-66886-R]
- DGRSDT [012/2000]
- Ministry of Higher Education and Scientific Research Government (MESRS) of Algeria
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Casein from ovine and bovine milk were hydrolyzed with two extracellular protease preparations from Lactobacillus brevis and Lactococcus lactis. The hydrolysates were analyzed by HPLC-MS/MS for peptide identification. A strain dependent peptide profile could be observed, regardless of the casein origin, and the specificity of these two proteases could be computationally ascribed. The cleavage pattern yielding phenylalanine, leucine, or tyrosine at C-terminal appeared both at L. lactis and Lb. brevis hydrolysates. However, the cleavage C-terminal to lysine was favored with Lb. brevis protease. The hydrolysates showed ACE-inhibitory activity with IC50 in the 16-70 mu g/mL range. Ovine casein hydrolysates yielded greater ACE-inhibitory activity. Previously described antihypertensive and opioid peptides were found in these ovine and bovine casein hydrolysates and prediction of the antihypertensive activity of the sequences based on quantitative structure and activity relationship (QSAR) was performed. This approach might represent a useful classification tool regarding health-related properties prior to further purification.
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