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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Format: | Article |
Language: | English |
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Elsevier
2022-01-01
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Series: | Current Research in Food Science |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S2665927122000958 |
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author | Olga Luisa Tavano Maria Julia de Miguel Amistá Giani Del Ciello Marilia Caroline Martini Rodrigues Amanda Marcela Bono Nishida Letícia Alves Valadares Bruno Moreira Siqueira Roseli Aparecida da Silva Gomes Marco Túlio Parolini Sinézio Inácio da Silva Junior |
author_facet | Olga Luisa Tavano Maria Julia de Miguel Amistá Giani Del Ciello Marilia Caroline Martini Rodrigues Amanda Marcela Bono Nishida Letícia Alves Valadares Bruno Moreira Siqueira Roseli Aparecida da Silva Gomes Marco Túlio Parolini Sinézio Inácio da Silva Junior |
author_sort | Olga Luisa Tavano |
collection | DOAJ |
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. |
first_indexed | 2024-04-11T14:19:18Z |
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id | doaj.art-9f3ed2c888074df7b90ad78ac18d6442 |
institution | Directory Open Access Journal |
issn | 2665-9271 |
language | English |
last_indexed | 2024-04-11T14:19:18Z |
publishDate | 2022-01-01 |
publisher | Elsevier |
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series | Current Research in Food Science |
spelling | doaj.art-9f3ed2c888074df7b90ad78ac18d64422022-12-22T04:19:07ZengElsevierCurrent Research in Food Science2665-92712022-01-01510281037Isolation and evaluation of quinoa (Chenopodium quinoa Willd.) protein fractions. A nutritional and bio-functional approach to the globulin fractionOlga Luisa Tavano0Maria Julia de Miguel Amistá1Giani Del Ciello2Marilia Caroline Martini Rodrigues3Amanda Marcela Bono Nishida4Letícia Alves Valadares5Bruno Moreira Siqueira6Roseli Aparecida da Silva Gomes7Marco Túlio Parolini8Sinézio Inácio da Silva Junior9ProThea – Research Group on Proteins for Health Promotion, Federal University of Alfenas, Minas, Gerais, Brazil; Corresponding author. Faculty of Nutrition, Federal University of Alfenas, 700 Gabriel Monteiro da Silva St, Alfenas, MG, 37130-000, Brazil.Nutrition Department, Triangulo Mineiro Federal University, Uberaba, Minas Gerais, BrazilNutrition Department, Triangulo Mineiro Federal University, Uberaba, Minas Gerais, BrazilNutrition Department, Triangulo Mineiro Federal University, Uberaba, Minas Gerais, BrazilNutrition Department, Triangulo Mineiro Federal University, Uberaba, Minas Gerais, BrazilNutrition Department, Triangulo Mineiro Federal University, Uberaba, Minas Gerais, BrazilProThea – Research Group on Proteins for Health Promotion, Federal University of Alfenas, Minas, Gerais, Brazil; Graduate Program in Nutrition and Longevity - PPGNL, Federal University of Alfenas, Minas Gerais, BrazilBiological and Natural Sciences Institute, Triangulo Mineiro Federal University, Uberaba, BrazilBiological and Natural Sciences Institute, Triangulo Mineiro Federal University, Uberaba, BrazilProThea – Research Group on Proteins for Health Promotion, Federal University of Alfenas, Minas, Gerais, BrazilThis 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.http://www.sciencedirect.com/science/article/pii/S2665927122000958GlobulinsProtein solubilityBioactive peptidesAntioxidant peptides |
spellingShingle | Olga Luisa Tavano Maria Julia de Miguel Amistá Giani Del Ciello Marilia Caroline Martini Rodrigues Amanda Marcela Bono Nishida Letícia Alves Valadares Bruno Moreira Siqueira Roseli Aparecida da Silva Gomes Marco Túlio Parolini Sinézio Inácio da Silva Junior Isolation and evaluation of quinoa (Chenopodium quinoa Willd.) protein fractions. A nutritional and bio-functional approach to the globulin fraction Current Research in Food Science Globulins Protein solubility Bioactive peptides Antioxidant peptides |
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 | Globulins Protein solubility Bioactive peptides Antioxidant peptides |
url | http://www.sciencedirect.com/science/article/pii/S2665927122000958 |
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