Antioxidant and angiotensin converting enzyme inhibitory activities of red lionfish (Pterois volitans L.) muscle protein hydrolysates obtained using pepsin-pancreatin system


Citation

Chuc-Koyoc, A. and Chel-Guerrero, L. and Sosa-Crespo, I. and Betancur-Ancona, D. and Vioque, J. and Gallegos-Tintoré, S. (2024) Antioxidant and angiotensin converting enzyme inhibitory activities of red lionfish (Pterois volitans L.) muscle protein hydrolysates obtained using pepsin-pancreatin system. International Food Research Journal (Malaysia), 31. pp. 215-227. ISSN 2231 7546

Abstract

Despite being an invasive species and representing a threat in the area, red lionfish (Pterois volitans L.) meat is valued for its pleasant taste and high protein content. The objective of the present work was to evaluate the angiotensin converting enzyme inhibition (ACE-I) and the antioxidant activities of red lionfish muscle protein hydrolysates in vitro. Hydrolysates were obtained using the pepsin-pancreatin system, and their degree of hydrolysis (DH), electrophoretic, and amino acid profile were determined. Subsequently, their ACE-I and ABTS+ radical scavenging activity were evaluated, selecting those with the highest response. The highest DH (66.1%) was found in the hydrolysate obtained at 120 min of reaction time (H120); electrophoresis revealed the action of the enzymes on the muscle proteins. The highest bioactivities occurred during hydrolysis with pepsin for 60 min (H60), obtaining the highest ACE-I of 68.8% (evaluated with 500 µg protein) with a DH of 16.8%, ACE-I related amino acid content of 33.6%, and hydrophobic amino acid content of 42.9%. With the 30 min hydrolysates (H30), the highest Trolox equivalent antioxidant capacity of 60.3 mM/mg protein was obtained with 18.4% DH and 22.1% radical scavenger amino acids; its comparison with H120 proved that higher DH did not produce a greater response in ABTS+ radical scavenging activity, DPPH, reducing power, and copper chelation assays; with β-carotene bleaching being the exception. Therefore, it can be concluded that red lionfish muscle hydrolysates could be a promising source of peptides with antihypertensive and antioxidant properties, and can be suitable as functional ingredients.


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Abstract

Despite being an invasive species and representing a threat in the area, red lionfish (Pterois volitans L.) meat is valued for its pleasant taste and high protein content. The objective of the present work was to evaluate the angiotensin converting enzyme inhibition (ACE-I) and the antioxidant activities of red lionfish muscle protein hydrolysates in vitro. Hydrolysates were obtained using the pepsin-pancreatin system, and their degree of hydrolysis (DH), electrophoretic, and amino acid profile were determined. Subsequently, their ACE-I and ABTS+ radical scavenging activity were evaluated, selecting those with the highest response. The highest DH (66.1%) was found in the hydrolysate obtained at 120 min of reaction time (H120); electrophoresis revealed the action of the enzymes on the muscle proteins. The highest bioactivities occurred during hydrolysis with pepsin for 60 min (H60), obtaining the highest ACE-I of 68.8% (evaluated with 500 µg protein) with a DH of 16.8%, ACE-I related amino acid content of 33.6%, and hydrophobic amino acid content of 42.9%. With the 30 min hydrolysates (H30), the highest Trolox equivalent antioxidant capacity of 60.3 mM/mg protein was obtained with 18.4% DH and 22.1% radical scavenger amino acids; its comparison with H120 proved that higher DH did not produce a greater response in ABTS+ radical scavenging activity, DPPH, reducing power, and copper chelation assays; with β-carotene bleaching being the exception. Therefore, it can be concluded that red lionfish muscle hydrolysates could be a promising source of peptides with antihypertensive and antioxidant properties, and can be suitable as functional ingredients.

Additional Metadata

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Item Type: Article
AGROVOC Term: Pterois volitans
AGROVOC Term: bioactive compounds
AGROVOC Term: antioxidants
AGROVOC Term: research
AGROVOC Term: electrophoresis
AGROVOC Term: pepsin
AGROVOC Term: protein hydrolysates
AGROVOC Term: nutritive value
AGROVOC Term: food quality
AGROVOC Term: functional foods
Geographical Term: Mexico
Uncontrolled Keywords: lionfish, peptides, hydrolysates, antioxidant, antihypertensive
Depositing User: Nor Hasnita Abdul Samat
Date Deposited: 29 Apr 2025 01:29
Last Modified: 29 Apr 2025 01:29
URI: http://webagris.upm.edu.my/id/eprint/1826

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