Isolation and Characterization of Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides from the Enzymatic Hydrolysate of Carapax Trionycis (the Shell of the Turtle Pelodiscus sinensis).
J Agric Food Chem
; 66(27): 7015-7022, 2018 Jul 11.
Article
in En
| MEDLINE
| ID: mdl-29916239
ABSTRACT
Carapax Trionycis (the shell of the turtle Pelodiscus sinensis) was hydrolyzed by six different commercial proteases. The hydrolysate prepared from papain showed stronger inhibitory activity against angiotensin I-converting enzyme (ACE) than other extracts. Two noncompetitive ACE inhibitory peptides were purified successively by ultrafiltration, gel filtration chromatography, ion exchange column chromatography, and high-performance liquid chromatography (HPLC). The amino acid sequences of them were identified as KRER and LHMFK, with IC50 values of 324.1 and 75.6 µM, respectively, confirming that Carapax Trionycis is a potential source of active peptides possessing ACE inhibitory activities. Besides, both enzyme kinetics and isothermal titration calorimetry (ITC) assay showed that LHMFK could form more stable complex with ACE than KRER, which is in accordance with the better inhibitory activity of LHMFK.
Key words
Full text:
1
Database:
MEDLINE
Main subject:
Peptides
/
Turtles
/
Angiotensin-Converting Enzyme Inhibitors
Limits:
Animals
Language:
En
Year:
2018
Type:
Article