ANGIOTENSIN I-CONVERTING ENZYME INHIBITORY AND ANTIOXIDANT PEPTIDE FRACTIONS FROM HARD-TO-COOK BEAN ENZYMATIC HYDROLYSATES
✍ Scribed by JORGE RUIZ-RUIZ; GLORIA DÁVILA-ORTÍZ; LUIS CHEL-GUERRERO; DAVID BETANCUR-ANCONA
- Book ID
- 111337915
- Publisher
- John Wiley and Sons
- Year
- 2011
- Tongue
- English
- Weight
- 322 KB
- Volume
- 37
- Category
- Article
- ISSN
- 0145-8884
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📜 SIMILAR VOLUMES
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
## Abstract **BACKGROUND:** Enzymatic proteolysis of food proteins is used to produce peptide fractions with the potential to act as physiological modulators. Fractionation of these proteins by ultrafiltration results in fractions rich in small peptides with the potential to act as functional food