Characterization of novel trypsin inhibitor in raw and toasted peanuts using a simple improved isolation
Trypsin inhibitors have been described in peanuts and their derived industrialized foods, demonstrating diversity and thermoresistance. Given their most varied applications, these enzymatic protease inhibitors have been isolated and characterized for their potential use as bioinsecticides, herbal me...
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ri-123456789-581312024-04-12T20:45:34Z Characterization of novel trypsin inhibitor in raw and toasted peanuts using a simple improved isolation Morais, Ana Heloneida de Araújo Maciel, Bruna Leal Lima Medeiros, Amanda Fernandes de Rocha, Maria Gabriela Ferreira Serquiz, Alexandre Coelho Machado, Richele Janaína Araújo Lima, Vanessa Cristina Oliveira Carvalho, Fabiana Maria Coimbra de Costa, Izael de Sousa Santos, Elizeu Antunes dos Arachis hypogaea L. Protein inhibitors Anti-trypsin activity Chromatography thermoresistance Bioactive protein Trypsin inhibitors have been described in peanuts and their derived industrialized foods, demonstrating diversity and thermoresistance. Given their most varied applications, these enzymatic protease inhibitors have been isolated and characterized for their potential use as bioinsecticides, herbal medicines, or medicines, but it is not simple. There are still no reports in the literature of the isolation and characterization of trypsin inhibitors in cultivar cavalo rosa (CCR) peanut, a common variety in Brazil. However, there are biological activities related to trypsin inhibitors from peanut-derived products. In this study, we isolated and characterized a novel trypsin inhibitor in CCR peanuts (Arachis hypogaea L.) under different processing conditions using a simple improved isolation. Raw and toasted peanut inhibitor was isolated by ammonium sulfate fractionation and trypsin-cyanogen bromide-activated SepharoseW 4B (CNBr-SepharoseW 4B) chromatography. The inhibitors from raw and toasted peanut were called AhTI1 and AhTI2, respectively, with potent anti-trypsin activity. Activity at different temperatures and pH was evaluated, and both samples were similarly stable under tested conditions. Minimum concentration for inhibition to occur (IC50) was 2.78 × 10−10 M and 2.39 × 10−10 M for AhTI1 and AhTI2, and inhibition constant (Ki) was 3.26 × 10−10 M and 1.54 × 10−10 M, respectively, showing non-competitive reversible kinetics. We concluded that AhTI1 and AhTI2 presented highly specific to trypsin and stable to toasting, different temperatures, and pH ranging. These are important characteristics in the process of developing bioinsecticides or biopharmaceuticals. Thus, this may be an interesting molecule, aiming at its biotechnological application, and it was obtained using a simple and easy isolation process 2024-04-12T20:45:33Z 2024-04-12T20:45:33Z 2019-06 article MEDEIROS, Amanda Fernandes de; ROCHA, Maria Gabriela Ferreira; SERQUIZ, Alexandre Coelho; MACHADO, Richele Janaína Araújo; LIMA, Vanessa Cristina Oliveira; CARVALHO, Fabiana Maria Coimbra de; COSTA, Izael de Sousa; MACIEL, Bruna Leal Lima; SANTOS, Elizeu Antunes dos; MORAIS, Ana Heloneida de Araújo. Characterization of novel trypsin inhibitor in raw and toasted peanuts using a simple improved isolation. Acta Chromatographica, [S.l.], v. 31, n. 2, p. 79-84, jun. 2019. DOI: 10.1556/1326.2017.00353. Disponível em: https://akjournals.com/view/journals/1326/31/2/article-p79.xml. Acesso em: 10 abr. 2024. https://repositorio.ufrn.br/handle/123456789/58131 http://dx.doi.org/10.1556/1326.2017.00353 en Attribution-NonCommercial 3.0 Brazil http://creativecommons.org/licenses/by-nc/3.0/br/ application/pdf Acta Chromatographica |
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RI - UFRN |
| language |
English |
| topic |
Arachis hypogaea L. Protein inhibitors Anti-trypsin activity Chromatography thermoresistance Bioactive protein |
| spellingShingle |
Arachis hypogaea L. Protein inhibitors Anti-trypsin activity Chromatography thermoresistance Bioactive protein Morais, Ana Heloneida de Araújo Maciel, Bruna Leal Lima Medeiros, Amanda Fernandes de Rocha, Maria Gabriela Ferreira Serquiz, Alexandre Coelho Machado, Richele Janaína Araújo Lima, Vanessa Cristina Oliveira Carvalho, Fabiana Maria Coimbra de Costa, Izael de Sousa Santos, Elizeu Antunes dos Characterization of novel trypsin inhibitor in raw and toasted peanuts using a simple improved isolation |
| description |
Trypsin inhibitors have been described in peanuts and their derived industrialized foods, demonstrating diversity and thermoresistance. Given their most varied applications, these enzymatic protease inhibitors have been isolated and characterized for their potential use as bioinsecticides, herbal medicines, or medicines, but it is not simple. There are still no reports in the literature of the isolation and characterization of trypsin inhibitors in cultivar cavalo rosa (CCR) peanut, a common variety in Brazil. However, there are biological activities related to trypsin inhibitors from peanut-derived products. In this study, we isolated and characterized a novel trypsin inhibitor in CCR peanuts (Arachis hypogaea L.) under different processing conditions using a simple improved isolation. Raw and toasted peanut inhibitor was isolated by ammonium sulfate fractionation and trypsin-cyanogen bromide-activated SepharoseW 4B (CNBr-SepharoseW 4B) chromatography. The inhibitors from raw and toasted peanut were called AhTI1 and AhTI2, respectively, with potent anti-trypsin activity. Activity at different temperatures and pH was evaluated, and both samples were similarly stable under tested conditions. Minimum concentration for inhibition to occur (IC50) was 2.78 × 10−10 M and 2.39 × 10−10 M for AhTI1 and AhTI2, and inhibition constant (Ki) was 3.26 × 10−10 M and 1.54 × 10−10 M, respectively, showing non-competitive reversible kinetics. We concluded that AhTI1 and AhTI2 presented highly specific to trypsin and stable to toasting, different temperatures, and pH ranging. These are important characteristics in the process of developing bioinsecticides or biopharmaceuticals. Thus, this may be an interesting molecule, aiming at its biotechnological application, and it was obtained using a simple and easy isolation process |
| format |
article |
| author |
Morais, Ana Heloneida de Araújo Maciel, Bruna Leal Lima Medeiros, Amanda Fernandes de Rocha, Maria Gabriela Ferreira Serquiz, Alexandre Coelho Machado, Richele Janaína Araújo Lima, Vanessa Cristina Oliveira Carvalho, Fabiana Maria Coimbra de Costa, Izael de Sousa Santos, Elizeu Antunes dos |
| author_facet |
Morais, Ana Heloneida de Araújo Maciel, Bruna Leal Lima Medeiros, Amanda Fernandes de Rocha, Maria Gabriela Ferreira Serquiz, Alexandre Coelho Machado, Richele Janaína Araújo Lima, Vanessa Cristina Oliveira Carvalho, Fabiana Maria Coimbra de Costa, Izael de Sousa Santos, Elizeu Antunes dos |
| author_sort |
Morais, Ana Heloneida de Araújo |
| title |
Characterization of novel trypsin inhibitor in raw and toasted peanuts using a simple improved isolation |
| title_short |
Characterization of novel trypsin inhibitor in raw and toasted peanuts using a simple improved isolation |
| title_full |
Characterization of novel trypsin inhibitor in raw and toasted peanuts using a simple improved isolation |
| title_fullStr |
Characterization of novel trypsin inhibitor in raw and toasted peanuts using a simple improved isolation |
| title_full_unstemmed |
Characterization of novel trypsin inhibitor in raw and toasted peanuts using a simple improved isolation |
| title_sort |
characterization of novel trypsin inhibitor in raw and toasted peanuts using a simple improved isolation |
| publisher |
Acta Chromatographica |
| publishDate |
2024 |
| url |
https://repositorio.ufrn.br/handle/123456789/58131 http://dx.doi.org/10.1556/1326.2017.00353 |
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| _version_ |
1797696622247804928 |