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Purification and characterization of angiotensin I-converting enzyme inhibitory peptide from enzymatic hydrolysates of Styela clava flesh tissue

✍ Scribed by Seok-Chun Ko; Jung-Kwon Lee; Hee-Guk Byun; Seung-Cheol Lee; You-Jin Jeon


Book ID
113862924
Publisher
Elsevier Science
Year
2012
Tongue
English
Weight
633 KB
Volume
47
Category
Article
ISSN
1873-3298

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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