Purification and characterization of angiotensin I converting enzyme inhibition peptides from sandworm Sipunculus nudus

Purification and characterization of angiotensin I converting enzyme inhibition peptides from... Three angiotensin I converting enzyme (ACE) inhibition peptides were isolated from sandworm Sipunculus nudus protein hydrolysate prepared using protamex. Consecutive purification methods, including size exclusion chromatography and reverse-phase high performance liquid chromatography (RP-HPLC), were used to isolate the ACE inhibition peptides. The amino acid sequences of the peptides were identified as Ile-Asn-Asp, Val-Glu-Pro-Gly and Leu-Ala-Asp-Glu-Phe. The IC50 values of the purified peptides for ACE inhibition activity were 34.72 μmol L−1, 20.55 μmol L−1 and 22.77 μmol L−1, respectively. These results suggested that S. nudus proteins contain specific peptides that can be released by enzymatic hydrolysis. This study may provide an experimental basis for further systematic research, rational development and clinical utilization of sandworm resources. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Ocean University of China Springer Journals

Purification and characterization of angiotensin I converting enzyme inhibition peptides from sandworm Sipunculus nudus

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Publisher
Science Press
Copyright
Copyright © 2017 by Science Press, Ocean University of China and Springer-Verlag GmbH Germany
Subject
Earth Sciences; Oceanography; Meteorology
ISSN
1672-5182
eISSN
1993-5021
D.O.I.
10.1007/s11802-017-3293-9
Publisher site
See Article on Publisher Site

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