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

Za izdvajanje bioaktivnih peptida iz kompas meduze (Chrysaora sp.) izoliran je kolagen, te je hidroliziran s pomoću tri proteaze: tripsina, alkalaze i komercijalnog prozivoda Protamex. Izmjeren je i uspoređen učinak različito inhibiranih peptida na inhibiciju angiotenzin konvertirajućeg enzima (ACE), te je pomoću metoda FRAP i DPPH ispitana njihova antioksidativna aktivnost. Osim toga, ispitan je utjecaj trajanja hidrolize na bioaktivnost peptida, tj. na inhibiciju ACE i antioksidativnu aktivnost. Najveća je ukupna antioksidacijska aktivnost (FRAP) izmjerena u hidrolizatima dobivenim pomoću komercijalne proteaze Protamex (25-27 mM) nakon 7 sati hidrolize, te nakon 9 sati hidrolize pomoću tripsina (24-26 mM). Nasuprot tome, hidrolizati dobiveni pomoću tripsina imali su najveću sposobnost uklanjanja DPPH radikala (94 % nakon 1 sata i 92 % nakon 3 sata). Hidrolizati dobiveni pomoću tripsina imali su najbolju sposobnost inhibicije ACE (89 % nakon 3 sata). Pomoću dvojne masene spektrometrije određene su sekvencije peptida koje su imale najveću aktivnost, a rezultati pokazuju da su hidrolizati imali veći udjel hidrofobnih aminokiselina i jedinstvenih sekvencija aminokiselina, što vjerojatno pridonosi njihovoj biološkoj aktivnosti.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 (25–27mM) 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