Details

Autor(en) / Beteiligte

• Barzideh, Zoha
• Latiff, Aishah Abd
• Gan, Chee-Yuen
• Abedin, Md Zainul
• Alias, Abd Karim

Titel

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

Ist Teil von

• Food technology and biotechnology, 2014-12, Vol.52 (4), p.495-504

Ort / Verlag

Croatia: Sveuciliste U Zagrebu

Erscheinungsjahr

2014

Link zum Volltext

Quelle

EBSCOhost Business Source Ultimate

Beschreibungen/Notizen

• Collagen isolated from the ribbon jellyfish ( sp.) was hydrolysed using three different proteases ( trypsin, alcalase and Protamex) to obtain bioactive peptides. Angiotensin-I-converting enzyme (ACE) inhibitory activity and antioxidant activities ( 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.