Amaranth Protein Hydrolysates Efficiently Reduce Systolic Blood Pressure in Spontaneously Hypertensive Rats
Alcalase is the enzyme of choice to release antihypertensive peptides from amaranth proteins, but the hydrolysis conditions have not been optimized yet. Furthermore, in vivo assays are needed to confirm such a hypotensive effect. Our aim was to optimize the hydrolysis of amaranth protein with alcala...
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MDPI AG
2017-11-01
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author | Giovanni Ramírez-Torres Noé Ontiveros Verónica Lopez-Teros Jesús Aurelio Ibarra-Diarte Cuauhtémoc Reyes-Moreno Edith Oliva Cuevas-Rodríguez Francisco Cabrera-Chávez |
author_facet | Giovanni Ramírez-Torres Noé Ontiveros Verónica Lopez-Teros Jesús Aurelio Ibarra-Diarte Cuauhtémoc Reyes-Moreno Edith Oliva Cuevas-Rodríguez Francisco Cabrera-Chávez |
author_sort | Giovanni Ramírez-Torres |
collection | DOAJ |
description | Alcalase is the enzyme of choice to release antihypertensive peptides from amaranth proteins, but the hydrolysis conditions have not been optimized yet. Furthermore, in vivo assays are needed to confirm such a hypotensive effect. Our aim was to optimize the hydrolysis of amaranth protein with alcalase and to test in vivo the hypotensive effect of the hydrolysates. A response surface analysis was carried out to optimize the hydrolysis reaction. The response variable was the Angiotensin Converting Enzyme (ACE-I) inhibition. The hydrolysis degree was determined (free alpha-amino groups measurement). The optimized hydrolysate bioavailability was assessed in the sera of mice and the hypotensive effect was assessed in spontaneously hypertensive rats. Control groups were administered captopril or water. The optimized hydrolysis conditions were: pH = 7.01, temperature = 52 °C, enzyme concentration 0.04 mU/mg, and time = 6.16 h. The optimized hydrolysate showed a 93.5% of ACE-I inhibition and a hydrolysis degree of 74.77%. After supplementation, the hydrolysate was bioavailable in mice from 5 to 60 min, and the hypotensive effect started at 4 h in spontaneously hypertensive rats (p < 0.05 vs. water group). This effect was similar to the captopril hypotensive effect for the next 3 h (p > 0.05). The use of amaranth-optimized hydrolysates as hypotensive supplements or ingredient for functional foods seems feasible. |
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spelling | doaj.art-b8fad4d1b26f4c1c853787043bc133452022-12-22T03:40:26ZengMDPI AGMolecules1420-30492017-11-012211190510.3390/molecules22111905molecules22111905Amaranth Protein Hydrolysates Efficiently Reduce Systolic Blood Pressure in Spontaneously Hypertensive RatsGiovanni Ramírez-Torres0Noé Ontiveros1Verónica Lopez-Teros2Jesús Aurelio Ibarra-Diarte3Cuauhtémoc Reyes-Moreno4Edith Oliva Cuevas-Rodríguez5Francisco Cabrera-Chávez6Nutritional Sciences, Department of Chemical and Biological Sciences, University of Sonora, Hermosillo, Sonora 83000, MexicoNutrition Sciences Academic Unit, University of Sinaloa, Culiacán, Sinaloa 80019, MexicoNutritional Sciences, Department of Chemical and Biological Sciences, University of Sonora, Hermosillo, Sonora 83000, MexicoNutrition Sciences Academic Unit, University of Sinaloa, Culiacán, Sinaloa 80019, MexicoFaculty of Chemical and Biological Sciences, University of Sinaloa, Culiacán, Sinaloa 80199, MexicoFaculty of Chemical and Biological Sciences, University of Sinaloa, Culiacán, Sinaloa 80199, MexicoFaculty of Physical Education and Sport, University of Sinaloa, Culiacán, Sinaloa 80019, MexicoAlcalase is the enzyme of choice to release antihypertensive peptides from amaranth proteins, but the hydrolysis conditions have not been optimized yet. Furthermore, in vivo assays are needed to confirm such a hypotensive effect. Our aim was to optimize the hydrolysis of amaranth protein with alcalase and to test in vivo the hypotensive effect of the hydrolysates. A response surface analysis was carried out to optimize the hydrolysis reaction. The response variable was the Angiotensin Converting Enzyme (ACE-I) inhibition. The hydrolysis degree was determined (free alpha-amino groups measurement). The optimized hydrolysate bioavailability was assessed in the sera of mice and the hypotensive effect was assessed in spontaneously hypertensive rats. Control groups were administered captopril or water. The optimized hydrolysis conditions were: pH = 7.01, temperature = 52 °C, enzyme concentration 0.04 mU/mg, and time = 6.16 h. The optimized hydrolysate showed a 93.5% of ACE-I inhibition and a hydrolysis degree of 74.77%. After supplementation, the hydrolysate was bioavailable in mice from 5 to 60 min, and the hypotensive effect started at 4 h in spontaneously hypertensive rats (p < 0.05 vs. water group). This effect was similar to the captopril hypotensive effect for the next 3 h (p > 0.05). The use of amaranth-optimized hydrolysates as hypotensive supplements or ingredient for functional foods seems feasible.https://www.mdpi.com/1420-3049/22/11/1905antihypertensive peptidesamaranthACE-I inhibition |
spellingShingle | Giovanni Ramírez-Torres Noé Ontiveros Verónica Lopez-Teros Jesús Aurelio Ibarra-Diarte Cuauhtémoc Reyes-Moreno Edith Oliva Cuevas-Rodríguez Francisco Cabrera-Chávez Amaranth Protein Hydrolysates Efficiently Reduce Systolic Blood Pressure in Spontaneously Hypertensive Rats Molecules antihypertensive peptides amaranth ACE-I inhibition |
title | Amaranth Protein Hydrolysates Efficiently Reduce Systolic Blood Pressure in Spontaneously Hypertensive Rats |
title_full | Amaranth Protein Hydrolysates Efficiently Reduce Systolic Blood Pressure in Spontaneously Hypertensive Rats |
title_fullStr | Amaranth Protein Hydrolysates Efficiently Reduce Systolic Blood Pressure in Spontaneously Hypertensive Rats |
title_full_unstemmed | Amaranth Protein Hydrolysates Efficiently Reduce Systolic Blood Pressure in Spontaneously Hypertensive Rats |
title_short | Amaranth Protein Hydrolysates Efficiently Reduce Systolic Blood Pressure in Spontaneously Hypertensive Rats |
title_sort | amaranth protein hydrolysates efficiently reduce systolic blood pressure in spontaneously hypertensive rats |
topic | antihypertensive peptides amaranth ACE-I inhibition |
url | https://www.mdpi.com/1420-3049/22/11/1905 |
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