Angiotensin-I-converting enzyme inhibitory peptides from tryptic hydrolysate of bovine αS2-casein
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چکیده
منابع مشابه
Short communication: bovine kappa-casein variants result in different angiotensin I converting enzyme (ACE) inhibitory peptides.
Proteins in bovine milk are a common source of bioactive peptides. The peptides are released by the digestion of caseins and whey proteins. Peptides derived from the different genetic variants A, B, C, E, F1, F2, G1, G2, H, I, and J of bovine kappa-casein (CSN3) were investigated for their inhibitory activities against angiotensin I converting enzyme (ACE). Amino acid sequences of the CSN3 vari...
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Introduction Many ACE inhibitory peptides have been isolated from various protein hydrolysates such as casein, soybean or fish protein. The purpose of this work is to isolate ACE inhibitory peptides derived from an enzymatic hydrolysate of fish by-products named Tensideal®, which is actually produced industrially by IDMER. The measurement of ACE inhibitory activity was performed using a HPLC me...
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متن کاملPeptides derived from Rhopilema esculentum hydrolysate exhibit angiotensin converting enzyme (ACE) inhibitory and antioxidant abilities.
Jellyfish (Rhopilema esculentum) was hydrolyzed using alcalase, and two peptides with angiotensin-I-converting enzyme (ACE) inhibitory and antioxidant activities were purified by ultrafiltration and consecutive chromatographic methods. The amino acid sequences of the two peptides were identified as VKP (342 Da) and VKCFR (651 Da) by electrospray ionization tandem mass spectrometry. The IC50 val...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 2002
ISSN: 0014-5793
DOI: 10.1016/s0014-5793(02)03576-7