Protein Hydrolysate Fractions from Sea Cucumber (Isostichopus badionotus) Inhibit Angiotensin-Converting Enzyme |
| |
Authors: | Yasser Chim-Chi Leticia Olivera-Castillo David Betancur-Ancona |
| |
Institution: | 1. Faculty of Chemical Engineering, Autonomous University of Yucatán, Mérida, Yucatan, Mexico;2. Center for Research and Advanced Studies of the National Polytechnic Institute, Mérida, Yucatán, México |
| |
Abstract: | Angiotensin-converting enzyme (ACE) inhibitory capacity was evaluated in hydrolysates from sea cucumber Isostichopus badionotus. The pepsin-pancreatin and Alcalase®-Flavorzyme® sequential systems were used. Hydrolysates were characterized in terms of degree of hydrolysis (DH), electrophoretic profile, and inhibitory activity. The Alcalase®-Flavorzyme® system produced hydrolysates with the highest DH, with that produced at 90 min exhibiting the highest ACE inhibitory action (86%). This hydrolysate was chosen for purification by ultrafiltration with five molecular weight cut-offs (< 1, 1–3, 3–5, 5–10, and > 10). The > 10-kDa fraction exhibited the highest ACE inhibitory action (80.7%) and was fractionated by gel fractionation chromatography. Of the 11 resulting fractions, IX had the highest ACE inhibitory action (73.4%) and lowest IC50 value (2-μg prot/mL). Hydrolysis of sea cucumber I. badionotus with the Alcalase®-Flavorzyme® system produced hydrolysates with ACE inhibitory action. These contained a peptide with an IC50 value comparable to those of synthetic ACE inhibitors. |
| |
Keywords: | Sea cucumber protein hydrolysates I-ECA protein fractions |
|
|