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Antioxidant, chelating, and angiotensin-converting enzyme inhibitory activities of peptide fractions from red lionfish (Pterois volitans L.) muscle protein hydrolysates.
- Source :
- International Food Research Journal; 2020, Vol. 27 Issue 2, p224-233, 10p
- Publication Year :
- 2020
-
Abstract
- Peptide fractions from marine animal hydrolysates can have biological activity. Red lionfish (Pterois volitans L.) is an invasive fish species in the tropical Atlantic, and harvest is a proposed control mechanism. With the aim of identifying possible bioactivity in peptides from red lionfish, an evaluation was done for the antioxidant, Cu2+ and Fe2+chelating, and angiotensin- converting enzyme inhibitory (ACE-I) activities of ultra-filtered peptide fractions derived from lionfish muscle enzymatically hydrolysed with the commercial enzyme Alcalase®. Hydrolysates were generated at 0, 30, 60, and 90 min, and the degree of hydrolysis (DH) were determined. The 30-min hydrolysate yielded the highest DH (30.78 ± 1.57%). This hydrolysate was ultra-filtered using four cut-offs (10, 5, 3, and 1 kDa), and the resulting polypeptides were analysed to generate their amino acids profile and estimated molecular weight (EMW). The F 5-3, F 3-1, and F < 1 kDa peptide fractions yielded the highest copper-chelating activity with values of approximately 88%. Fractions F > 10 and F 10-5 kDa yielded the highest iron-chelating activity with values of approximately 18.8%. The β-carotene bleaching test showed that the F 10-5, F 5-3, F 3-1, and F < 1 kDa fractions to have high antioxidant capacity, inhibiting more than 80% of β-carotene discoloration versus the control. The F 5-3 kDa fraction exhibited the highest ACE inhibition (34.57%), possibly due to the presence of amino acids such as Gly, Leu, Phe, Tyr, and Pro. Polypeptides with an EMW of 6.51 to 3.49 kDa were identified in F > 10, and 2.17 kDa in F 5-3. Peptide fractions from hydrolysed red lionfish muscle exhibit in vitro activities, and could serve as potential source of functional ingredients. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 19854668
- Volume :
- 27
- Issue :
- 2
- Database :
- Complementary Index
- Journal :
- International Food Research Journal
- Publication Type :
- Academic Journal
- Accession number :
- 143521367