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
QIGLF, a novel angiotensin I-converting enzyme-inhibitory peptide from egg white protein
✍ Scribed by Zhipeng Yu; Wenzhu Zhao; Jingbo Liu; Jing Lu; Feng Chen
- Publisher
- John Wiley and Sons
- Year
- 2011
- Tongue
- English
- Weight
- 250 KB
- Volume
- 91
- Category
- Article
- ISSN
- 0022-5142
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
Acetes chinensis is an underutilized shrimp species thriving in the Bo Hai Gulf of China. In a previous study, we had used the protease from Bacillus sp. SM98011 to digest this kind of shrimp and found that the oligopeptide-enriched hydrolysate possessed antioxidant activity and high angiotensin I-c
## Abstract Angiotensin I‐converting enzyme (ACE) inhibitory peptide was isolated from wheat gliadin hydrolysate prepared with acid protease. Consecutive purification methods were used for peptide isolation including ion‐exchange chromatography, size‐exclusion chromatography, and reverse‐phase high
## Abstract In this report, we present the use of CE‐MS as complement to RP separation for the identification of novel angiotensin‐converting enzyme‐inhibitory (ACEI) peptides from a complex milk protein hydrolysate. As preliminary step, fast protein LC (FPLC) was used to isolate the different case