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Isolation and evaluation of quinoa (Chenopodium quinoa Willd.) protein fractions. A nutritional and bio-functional approach to the globulin fraction

This study evaluated the solubility profiles of quinoa grain proteins and applied a complete process for the isolation of its main protein fractions, namely: albumins, globulins, prolamins and glutelins, which corresponded to 26.96%, 41.3%, 1.7% and 23.16% of the total protein content, respectively....

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Autores principales: Tavano, Olga Luisa, Amistá, Maria Julia de Miguel, Del Ciello, Giani, Rodrigues, Marilia Caroline Martini, Bono Nishida, Amanda Marcela, Valadares, Letícia Alves, Siqueira, Bruno Moreira, Gomes, Roseli Aparecida da Silva, Parolini, Marco Túlio, Silva Junior, Sinézio Inácio da
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9234336/
https://www.ncbi.nlm.nih.gov/pubmed/35769315
http://dx.doi.org/10.1016/j.crfs.2022.06.006
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author Tavano, Olga Luisa
Amistá, Maria Julia de Miguel
Del Ciello, Giani
Rodrigues, Marilia Caroline Martini
Bono Nishida, Amanda Marcela
Valadares, Letícia Alves
Siqueira, Bruno Moreira
Gomes, Roseli Aparecida da Silva
Parolini, Marco Túlio
Silva Junior, Sinézio Inácio da
author_facet Tavano, Olga Luisa
Amistá, Maria Julia de Miguel
Del Ciello, Giani
Rodrigues, Marilia Caroline Martini
Bono Nishida, Amanda Marcela
Valadares, Letícia Alves
Siqueira, Bruno Moreira
Gomes, Roseli Aparecida da Silva
Parolini, Marco Túlio
Silva Junior, Sinézio Inácio da
author_sort Tavano, Olga Luisa
collection PubMed
description This study evaluated the solubility profiles of quinoa grain proteins and applied a complete process for the isolation of its main protein fractions, namely: albumins, globulins, prolamins and glutelins, which corresponded to 26.96%, 41.3%, 1.7% and 23.16% of the total protein content, respectively. When these fractions were digested with pepsin followed by pancreatin, the degrees of hydrolysis achieved varied between 26.62% (for unheated globulin fraction) and 38.97% (for unheated glutelin), with casein reached 33.73% hydrolysis. After heating, the globulin hydrolysis degree increased to 34.7%, not significantly differing from casein. These results reflect its good susceptibility to hydrolysis by digestive enzymes, and this observation is reinforced with assays with pepsin, trypsin and chymotrypsin tested separately. Globulins, the largest protein fraction, showed promising results in additional assays regarding the amino acid profile, with limitation only for lysine in relation to the FAO standard, and the potential for releasing bioactive peptides after digestion. Although pepsin-digested globulin inhibited only 5% of ACE activity under the conditions tested, after 24h with the addition of pancreatin, the inhibition was 100%. Antioxidant activity (DPPH assay) also indicated very similar results, when hydrolysis with pepsin was inefficient in releasing antioxidant peptides, while hydrolysis by pancreatin led to 35 times greater results.
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spelling pubmed-92343362022-06-28 Isolation and evaluation of quinoa (Chenopodium quinoa Willd.) protein fractions. A nutritional and bio-functional approach to the globulin fraction Tavano, Olga Luisa Amistá, Maria Julia de Miguel Del Ciello, Giani Rodrigues, Marilia Caroline Martini Bono Nishida, Amanda Marcela Valadares, Letícia Alves Siqueira, Bruno Moreira Gomes, Roseli Aparecida da Silva Parolini, Marco Túlio Silva Junior, Sinézio Inácio da Curr Res Food Sci Research Paper This study evaluated the solubility profiles of quinoa grain proteins and applied a complete process for the isolation of its main protein fractions, namely: albumins, globulins, prolamins and glutelins, which corresponded to 26.96%, 41.3%, 1.7% and 23.16% of the total protein content, respectively. When these fractions were digested with pepsin followed by pancreatin, the degrees of hydrolysis achieved varied between 26.62% (for unheated globulin fraction) and 38.97% (for unheated glutelin), with casein reached 33.73% hydrolysis. After heating, the globulin hydrolysis degree increased to 34.7%, not significantly differing from casein. These results reflect its good susceptibility to hydrolysis by digestive enzymes, and this observation is reinforced with assays with pepsin, trypsin and chymotrypsin tested separately. Globulins, the largest protein fraction, showed promising results in additional assays regarding the amino acid profile, with limitation only for lysine in relation to the FAO standard, and the potential for releasing bioactive peptides after digestion. Although pepsin-digested globulin inhibited only 5% of ACE activity under the conditions tested, after 24h with the addition of pancreatin, the inhibition was 100%. Antioxidant activity (DPPH assay) also indicated very similar results, when hydrolysis with pepsin was inefficient in releasing antioxidant peptides, while hydrolysis by pancreatin led to 35 times greater results. Elsevier 2022-06-20 /pmc/articles/PMC9234336/ /pubmed/35769315 http://dx.doi.org/10.1016/j.crfs.2022.06.006 Text en © 2022 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research Paper
Tavano, Olga Luisa
Amistá, Maria Julia de Miguel
Del Ciello, Giani
Rodrigues, Marilia Caroline Martini
Bono Nishida, Amanda Marcela
Valadares, Letícia Alves
Siqueira, Bruno Moreira
Gomes, Roseli Aparecida da Silva
Parolini, Marco Túlio
Silva Junior, Sinézio Inácio da
Isolation and evaluation of quinoa (Chenopodium quinoa Willd.) protein fractions. A nutritional and bio-functional approach to the globulin fraction
title Isolation and evaluation of quinoa (Chenopodium quinoa Willd.) protein fractions. A nutritional and bio-functional approach to the globulin fraction
title_full Isolation and evaluation of quinoa (Chenopodium quinoa Willd.) protein fractions. A nutritional and bio-functional approach to the globulin fraction
title_fullStr Isolation and evaluation of quinoa (Chenopodium quinoa Willd.) protein fractions. A nutritional and bio-functional approach to the globulin fraction
title_full_unstemmed Isolation and evaluation of quinoa (Chenopodium quinoa Willd.) protein fractions. A nutritional and bio-functional approach to the globulin fraction
title_short Isolation and evaluation of quinoa (Chenopodium quinoa Willd.) protein fractions. A nutritional and bio-functional approach to the globulin fraction
title_sort isolation and evaluation of quinoa (chenopodium quinoa willd.) protein fractions. a nutritional and bio-functional approach to the globulin fraction
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9234336/
https://www.ncbi.nlm.nih.gov/pubmed/35769315
http://dx.doi.org/10.1016/j.crfs.2022.06.006
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