Citas bibligráficas
Escobar, N., (2023). Evaluación de la proteína de la quinua (Chenopodium quinua Willd.) como fuente de péptidos bioactivos mediante proteólisis in silico [Universidad Nacional Agraria La Molina]. https://hdl.handle.net/20.500.12996/6173
Escobar, N., Evaluación de la proteína de la quinua (Chenopodium quinua Willd.) como fuente de péptidos bioactivos mediante proteólisis in silico []. PE: Universidad Nacional Agraria La Molina; 2023. https://hdl.handle.net/20.500.12996/6173
@misc{renati/1115207,
title = "Evaluación de la proteína de la quinua (Chenopodium quinua Willd.) como fuente de péptidos bioactivos mediante proteólisis in silico",
author = "Escobar Mendoza, Nicolle Sandy",
publisher = "Universidad Nacional Agraria La Molina",
year = "2023"
}
Quinoa is an Andean grain, well known for the nutritional quality and biological properties of its protein. Thus, the present investigation evaluated the potential of quinoa globulin protein as a precursor of peptides with inhibitory activities of the angiotensin I converting enzyme (ACE) (antihypertensive effect) and of the enzyme dipeptidyl peptidase IV (DPP-IV) (hypoglycemic effect) using in silico and in vitro approaches. The thermolysin enzyme was used for the evaluation of the in silico hydrolysis of the globulins: 13S globulin seed storage protein 2-like, 13S globulin seed storage protein 1-like, 11S globulin seed storage protein 2-like and 11S seed storage, using the BIOPEP database. After hydrolysis, using the PeptideRanker program, it was selected, among all the peptides generated from hydrolysis, to three of them: FPR (Phenylalanine-Proline-Arginine), YSPHW (Tyrosine-Serine-Proline-Histidine-Tryptophan) and IPPG (Isoleucine-Proline-Proline-Glycine), as peptides with bioactivity of interest for their antihypertensive and/or hypoglycemic effects. The three peptides were subsequently evaluated in silico for their stability against gastrointestinal digestion conditions (using pepsin, trypsin and chymotrypsin, sequentially), finding that FPR and YSPHW undergo hydrolysis, obtaining smaller peptides: PR and SPH, respectively; while the IPPG peptide remained intact; additionally, it was observed that the first one stood out for its ACE inhibitory activity, the second for its DPP-IV inhibitory activity and the last one stands out for both activities; results that were evaluated by molecular docking analysis (docking) in silico, where the findings found were supported The results found from the in silico analysis were later corroborated by in vitro evaluation carried out on a protein concentrate and on the quinoa globulin fraction , hydrolyzed with thermolysin. The results of this research indicate that the globulin fraction of quinoa hydrolyzed with thermolysin can be considered a very good source for obtaining antihypertensive and hypoglycemic peptides.
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