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Effect of angiotensin I-converting enzyme (ACE) inhibitory peptide purified from enzymatic hydrolysates ofStyela plicata

✍ Scribed by Seok-Chun Ko; Min Cheol Kang; Jung-Kwon Lee; Hee-Guk Byun; Se-Kwon Kim; Seung-Cheol Lee; Byong-Tae Jeon; Pyo-Jam Park; Won-Kyo Jung; You-Jin Jeon

Publisher
Springer
Year
2011
Tongue
English
Weight
298 KB
Volume
233
Category
Article
ISSN
0044-3026

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## 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

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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