Characterization of novel trypsin inhibitor in raw and toasted peanuts using a simple improved isolation

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dc.contributor.authorMorais, Ana Heloneida de Araújo
dc.contributor.authorMaciel, Bruna Leal Lima
dc.contributor.authorMedeiros, Amanda Fernandes de
dc.contributor.authorRocha, Maria Gabriela Ferreira
dc.contributor.authorSerquiz, Alexandre Coelho
dc.contributor.authorMachado, Richele Janaína Araújo
dc.contributor.authorLima, Vanessa Cristina Oliveira
dc.contributor.authorCarvalho, Fabiana Maria Coimbra de
dc.contributor.authorCosta, Izael de Sousa
dc.contributor.authorSantos, Elizeu Antunes dos
dc.date.accessioned2024-04-12T20:45:33Z
dc.date.available2024-04-12T20:45:33Z
dc.date.issued2019-06
dc.description.resumoTrypsin 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 processpt_BR
dc.identifier.citationMEDEIROS, 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.pt_BR
dc.identifier.doihttp://dx.doi.org/10.1556/1326.2017.00353
dc.identifier.urihttps://repositorio.ufrn.br/handle/123456789/58131
dc.languageenpt_BR
dc.publisherActa Chromatographicapt_BR
dc.rightsAttribution-NonCommercial 3.0 Brazil*
dc.rights.urihttp://creativecommons.org/licenses/by-nc/3.0/br/*
dc.subjectArachis hypogaea L.pt_BR
dc.subjectProtein inhibitorspt_BR
dc.subjectAnti-trypsin activitypt_BR
dc.subjectChromatography thermoresistancept_BR
dc.subjectBioactive proteinpt_BR
dc.titleCharacterization of novel trypsin inhibitor in raw and toasted peanuts using a simple improved isolationpt_BR
dc.typearticlept_BR

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