ACE Inhibitory and Antioxidant Activities of Collagen Hydrolysates from the Ribbon Jellyfish (Chrysaora sp.)
| Autor: | Abd Karim Alias, Aishah Latiff, Md. Zainul Abedin, Chee-Yuen Gan, Zoha Barzideh |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Antioxidant
DPPH General Chemical Engineering medicine.medical_treatment lcsh:Biotechnology Peptide Industrial and Manufacturing Engineering Hydrolysate chemistry.chemical_compound collagen and protein hydrolysates DPPH and FRAP lcsh:TP248.13-248.65 medicine chemistry.chemical_classification ACE inhibition antihypertensive and antioxidant activity Chrysaora sp jellyfish lcsh:TP368-456 Biological activity Trypsin kolagen i hidrolizati proteina inhibicija ACE antihipertenzijski učinak i antioksidativna aktivnost DPPH i FRAP meduza Amino acid lcsh:Food processing and manufacture Enzyme chemistry Biochemistry Food Science Biotechnology medicine.drug |
| Zdroj: | Food Technology and Biotechnology, Vol 52, Iss 4, Pp 495-504 (2014) Food Technology and Biotechnology Volume 52 Issue 4 |
| ISSN: | 1334-2606 1330-9862 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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