ACE Inhibitory and Antioxidant Activities of Collagen Hydrolysates from the Ribbon Jellyfi sh (Chrysaora sp.)
Collagen isolated from the ribbon jellyfi sh (Chrysaora sp.) was hydrolysed using three diff erent proteases (i.e. trypsin, alcalase and Protamex) to obtain bioactive peptides. Angiotensin- I-converting enzyme (ACE) inhibitory activity and antioxidant activities (i.e. ferric reducing antioxidant...
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
University of Zagreb
2014
|
| Subjects: | |
| Online Access: | http://eprints.usm.my/38239/ http://eprints.usm.my/38239/1/ACE_Inhibitory_and_Antioxidant_Activities_of_Collagen_Hydrolysates.pdf |
| Summary: | Collagen isolated from the ribbon jellyfi sh (Chrysaora sp.) was hydrolysed using three
diff erent proteases (i.e. trypsin, alcalase and Protamex) to obtain bioactive peptides. Angiotensin-
I-converting enzyme (ACE) inhibitory activity and antioxidant activities (i.e. ferric
reducing antioxidant power (FRAP) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical
scavenging activity) of the peptides were measured and compared, and the eff ect of the
duration of hydrolysis on the bioactivity (ACE inhibitory and antioxidant activities) of
peptides was also evaluated. FRAP activity was the highest in Protamex-induced (25–27
mM) and trypsin-induced hydrolysates (24–26 mM) at 7 and 9 h, respectively. Conversely,
hydrolysates produced by trypsin for 1 and 3 h showed the highest DPPH radical scavenging
activities (94 and 92 %, respectively). Trypsin-induced hydrolysates (at 3 h) also showed
the highest ACE inhibitory activity (89 %). The peptide sequences with the highest activities
were identifi ed using tandem mass spectrometry, and the results show that the hydrolysates
had a high content of hydrophobic amino acids as well as unique amino acid sequences,
which likely contribute to their biological activities. |
|---|