Isolation of Peptides with Angiotensin I-converting Enzyme Inhibitory Effect Derived from Hydrolysate of Upstream Chum Salmon Muscle
β Scribed by S. Ono; M. Hosokawa; K. Miyashita; K. Takahashi
- Book ID
- 108825210
- Publisher
- Institute of Food Technologists
- Year
- 2003
- Tongue
- English
- Weight
- 264 KB
- Volume
- 68
- Category
- Article
- ISSN
- 0022-1147
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract Angiotensin Iβconverting enzyme (ACE) inhibitory peptide was isolated from wheat gliadin hydrolysate prepared with acid protease. Consecutive purification methods were used for peptide isolation including ionβexchange chromatography, sizeβexclusion chromatography, and reverseβphase high
Mung bean protein isolates were hydrolyzed for 2 h by Alcalase. The generated hydrolysate showed angiotensin I-converting enzyme (ACE) inhibitory activity with the IC(50) value of 0.64 mg protein/ml. Three kinds of novel ACE inhibitory peptides were isolated from the hydrolysate by Sephadex G-15 and