getpdf https://doi.org/10.17113/ftb.52.04.14.3641

 

ACE Inhibitory and Antioxidant Activities of Collagen Hydrolysates from the Ribbon Jellyfish (Chrysaora sp.)

Zoha Barzideh1,2*, Aishah Abd Latiff 3, Chee-Yuen Gan2, Md. Zainul Abedin1 and Abd Karim Alias1


1
Food Technology Division, School of Industrial Technology, Universiti Sains Malaysia, 11800 Minden, Penang, Malaysia

2Centre for Advanced Analytical Toxicology Services, Universi ti Sains Malaysia, 11800 Minden, Penang, Malaysia
3Toxicology and Multipurpose Laboratory, Anti Doping Laboratory Qatar, Doha, Qatar

Article history
:

Received March 11, 2014
Accepted September 17, 2014

Key words
:

collagen, protein hydrolysates, ACE inhibition, antihypertensive activity, antioxidant activity, DPPH, FRAP, Chrysaora sp., jellyfish

Summary:

Collagen isolated from the ribbon jellyfish (Chrysaora sp.) was hydrolysed using three different 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 effect 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 identified 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.

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