Amaranth proteins emulsions as delivery system of Angiotensin-I converting enzyme inhibitory peptides
We analyze the possibility of using the emulsifying properties of amaranth proteins and the bioactivity shown by peptide sequences encrypted in these proteins to formulate functional emulsions with angiotensin I-converting enzyme (ACE) inhibitory activity. For this we formulate O:W emulsions, 20:80,...
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I19-R120-10915-1523352023-05-02T20:08:05Z http://sedici.unlp.edu.ar/handle/10915/152335 issn:0268-005X Amaranth proteins emulsions as delivery system of Angiotensin-I converting enzyme inhibitory peptides Suárez, Santiago Emmanuel Añón, María Cristina 2019-05 2023-05-02T14:05:59Z en Ciencias Exactas Química Amaranth proteins O:W emulsions Antihypertensive deliver Functional foods We analyze the possibility of using the emulsifying properties of amaranth proteins and the bioactivity shown by peptide sequences encrypted in these proteins to formulate functional emulsions with angiotensin I-converting enzyme (ACE) inhibitory activity. For this we formulate O:W emulsions, 20:80, from a mixture in equal parts (50:50) of amaranth protein isolates (API), and hydrolysates (AH) at 1 and 2% protein w/v. Results obtained showed that these emulsions, API50-AH50-1% and API50-AH50-2%, are highly flocculated (Flocculation index: 8.2 and 5.9) and stable at least for 8 days, without evident creaming or coalescence. The components present in the emulsions were capable of inhibiting ACE, in in vitro assays (IC₅₀ of 0.14 ± 0.02 mg/mL). API and API50-AH50 emulsions were subjected to a simulated gastrointestinal digestion in vitro. The emulsions were susceptible to aggregation and coalescence phenomena during this process, which could be a consequence of the chaotropic action of the bile salt on the interface and the proteolytic and lipolytic action of pancreatin and lipase, respectively (D₄.₃ of original emulsion: 1.22 ± 0.01 μm and D₄.₃ of digested emulsion 79.5 ± 17.1 μm). We also found that amaranth proteins were more resistant to gastric than duodenal digestion. After the process of simulated gastrointestinal digestion, the inhibition of ACE (IC₅₀ of 0.13 ± 0.07 mg/mL) was maintained. This fact evidences the protective effect of the emulsion on the bioavailability of the ACE inhibitory peptides, by either their participation in the formation of the interfacial film and/or their participation in the network of formed flocs. Centro de Investigación y Desarrollo en Criotecnología de Alimentos Articulo Articulo http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) application/pdf 154-161 |
institution |
Universidad Nacional de La Plata |
institution_str |
I-19 |
repository_str |
R-120 |
collection |
SEDICI (UNLP) |
language |
Inglés |
topic |
Ciencias Exactas Química Amaranth proteins O:W emulsions Antihypertensive deliver Functional foods |
spellingShingle |
Ciencias Exactas Química Amaranth proteins O:W emulsions Antihypertensive deliver Functional foods Suárez, Santiago Emmanuel Añón, María Cristina Amaranth proteins emulsions as delivery system of Angiotensin-I converting enzyme inhibitory peptides |
topic_facet |
Ciencias Exactas Química Amaranth proteins O:W emulsions Antihypertensive deliver Functional foods |
description |
We analyze the possibility of using the emulsifying properties of amaranth proteins and the bioactivity shown by peptide sequences encrypted in these proteins to formulate functional emulsions with angiotensin I-converting enzyme (ACE) inhibitory activity. For this we formulate O:W emulsions, 20:80, from a mixture in equal parts (50:50) of amaranth protein isolates (API), and hydrolysates (AH) at 1 and 2% protein w/v. Results obtained showed that these emulsions, API50-AH50-1% and API50-AH50-2%, are highly flocculated (Flocculation index: 8.2 and 5.9) and stable at least for 8 days, without evident creaming or coalescence. The components present in the emulsions were capable of inhibiting ACE, in in vitro assays (IC₅₀ of 0.14 ± 0.02 mg/mL).
API and API50-AH50 emulsions were subjected to a simulated gastrointestinal digestion in vitro. The emulsions were susceptible to aggregation and coalescence phenomena during this process, which could be a consequence of the chaotropic action of the bile salt on the interface and the proteolytic and lipolytic action of pancreatin and lipase, respectively (D₄.₃ of original emulsion: 1.22 ± 0.01 μm and D₄.₃ of digested emulsion 79.5 ± 17.1 μm). We also found that amaranth proteins were more resistant to gastric than duodenal digestion.
After the process of simulated gastrointestinal digestion, the inhibition of ACE (IC₅₀ of 0.13 ± 0.07 mg/mL) was maintained. This fact evidences the protective effect of the emulsion on the bioavailability of the ACE inhibitory peptides, by either their participation in the formation of the interfacial film and/or their participation in the network of formed flocs. |
format |
Articulo Articulo |
author |
Suárez, Santiago Emmanuel Añón, María Cristina |
author_facet |
Suárez, Santiago Emmanuel Añón, María Cristina |
author_sort |
Suárez, Santiago Emmanuel |
title |
Amaranth proteins emulsions as delivery system of Angiotensin-I converting enzyme inhibitory peptides |
title_short |
Amaranth proteins emulsions as delivery system of Angiotensin-I converting enzyme inhibitory peptides |
title_full |
Amaranth proteins emulsions as delivery system of Angiotensin-I converting enzyme inhibitory peptides |
title_fullStr |
Amaranth proteins emulsions as delivery system of Angiotensin-I converting enzyme inhibitory peptides |
title_full_unstemmed |
Amaranth proteins emulsions as delivery system of Angiotensin-I converting enzyme inhibitory peptides |
title_sort |
amaranth proteins emulsions as delivery system of angiotensin-i converting enzyme inhibitory peptides |
publishDate |
2019 |
url |
http://sedici.unlp.edu.ar/handle/10915/152335 |
work_keys_str_mv |
AT suarezsantiagoemmanuel amaranthproteinsemulsionsasdeliverysystemofangiotensiniconvertingenzymeinhibitorypeptides AT anonmariacristina amaranthproteinsemulsionsasdeliverysystemofangiotensiniconvertingenzymeinhibitorypeptides |
_version_ |
1765660108880084992 |