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Mar. Drugs 2017, 15(10), 311; https://doi.org/10.3390/md15100311

Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity, Antioxidant Properties, Phenolic Content and Amino Acid Profiles of Fucus spiralis L. Protein Hydrolysate Fractions

1
Biotechnology Centre of Azores (CBA), University of Azores, 9501-801 Ponta Delgada, Portugal
2
Research Center for Agricultural Technology (CITA-A), University of Azores, 9501-801 Ponta Delgada, Portugal
3
Azorean Biodiversity Group, Centre for Ecology, Evolution and Environmental Changes (CE3C), Department of Biology, University of Azores, 9501-801 Ponta Delgada, Portugal
*
Author to whom correspondence should be addressed.
Received: 2 September 2017 / Revised: 29 September 2017 / Accepted: 9 October 2017 / Published: 13 October 2017
(This article belongs to the Special Issue Development and Application of Herbal Medicine from Marine Origin)
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Abstract

Food protein-derived hydrolysates with multi-bioactivities such as antihypertensive and antioxidant properties have recently received special attention since both activities can play significant roles in preventing cardiovascular diseases. This study reports, for the first time, the angiotensin I-converting enzyme (ACE)-inhibition and antioxidant properties of ultrafiltrate fractions (UF) with different molecular weight ranges (<1, 1–3 and ≥3 kDa) obtained from Fucus spiralis protein hydrolysate (FSPH) digested with cellulase–bromelain. The amino acids profile, recovery yield, protein, peptide and total phenolic contents of these FSPH-UF, and the in vitro digestibility of F. spiralis crude protein were also investigated. FSPH-UF ≥3 kDa presented remarkably higher ACE-inhibition, yield, peptide and polyphenolic (phlorotannins) contents. Antioxidant analysis showed that FSPH-UF <1 kDa and ≥3 kDa exhibited significantly higher scavenging of 2,2-diphenyl-1-picrylhydrazyl radical and ferrous ion-chelating (FIC) activity. FSPH-UF ≥3 kDa had also notably higher ferric reducing antioxidant power (FRAP). Strong correlations were observed between ACE-inhibition and antioxidant activities (FIC and FRAP). The results suggest that ACE-inhibition and antioxidant properties of FSPH-UF may be due to the bioactive peptides and polyphenols released during the enzymatic hydrolysis. In conclusion, this study shows the potential use of defined size FSPH-UF for the prevention/treatment of hypertension and/or oxidative stress-related diseases. View Full-Text
Keywords: edible brown algae; protein enzymatic hydrolysate; ultrafiltration; ACE-inhibition; antioxidant properties; phlorotannins; peptide fractions; amino acids composition; marine functional foods; cardiovascular-health edible brown algae; protein enzymatic hydrolysate; ultrafiltration; ACE-inhibition; antioxidant properties; phlorotannins; peptide fractions; amino acids composition; marine functional foods; cardiovascular-health
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
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Paiva, L.; Lima, E.; Neto, A.I.; Baptista, J. Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity, Antioxidant Properties, Phenolic Content and Amino Acid Profiles of Fucus spiralis L. Protein Hydrolysate Fractions. Mar. Drugs 2017, 15, 311.

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