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Navegando por Autor "Lima, Vanessa Cristina Oliveira"

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    Artigo
    Atividade hemaglutinante em sementes exóticas germinadas e comestíveis
    (Revista Brasileira de Inovação Tecnológica em Saúde, 2017-04) Morais, Ana Heloneida de Araújo; Lima, Vanessa Cristina Oliveira; Silva, Priscila Fabíola dos Santos; Alves, Nínive Rayane de Medeiros; Pereira, Danielle Alves de Oliveira; Figueredo, Júlia Braga dos Santos; Costa, Izael de Sousa; Carvalho, Fabiana Maria Coimbra de; Santos, Elizeu Antunes dos
    As sementes não convencionais vêm ganhando destaque no cenário alimentar pela alegação de que são benéficas à saúde; concomitante a esse fato, o consumo das sementes altera seu metabolismo e sua composição, fato relacionado, segundo a literatura, a uma maior síntese e menor degradação de aglutininas. O objetivo deste estudo constituiu em avaliar a atividade hemaglutinante nos extratos totais aquosos de sementes exóticas germinadas e comestíveis. Assim, foram testadas a atividade hemaglutinante, a dependência de íons e a inibição por carboidratos dos extratos dessas sementes. Como resultado, para as sementes estudadas, identificou-se a presença de aglutininas em todas as sementes germinadas, sendo mais expressivas nas sementes de Gergelim (88,11 UH/mg) e Girassol (61,07 UH/mg) e nas sementes não germinadas, apenas não apresentaram atividade hemaglutinante, as de Quinoa, Feijão Mungo e Gergelim. A especificidade para os tipos sanguíneos (AB0), tratado com papaína ou tripsina variaram entre as sementes, bem como a dependência por e íons magnésio e cálcio, atentando para a necessidade crescente de estudos mais aprofundados sobre fatores antinutricionais em alimentos alternativos e sementes germinadas
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    Artigo
    Characterization of novel trypsin inhibitor in raw and toasted peanuts using a simple improved isolation
    (Acta Chromatographica, 2019-06) 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
    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
  • Nenhuma Miniatura disponível
    Artigo
    Characterization of novel trypsin inhibitor in raw and toasted peanuts using a simple improved isolation
    (Acta Chromatographica, 2019-06) 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; Morais, Ana Heloneida de Araújo
    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
  • Nenhuma Miniatura disponível
    Artigo
    Supplementation with a new trypsin inhibitor from peanut is associated with reduced fasting glucose, weight control, and increased plasma CCK secretion in an animal model
    (Journal of Enzyme Inhibition and Medicinal Chemistry, 2016-02) Maciel, Bruna Leal Lima; Serquiz, Alexandre Coelho; Machado, Richele Janaína de Araújo; Serquiz, Raphael Paschoal; Lima, Vanessa Cristina Oliveira; Carvalho, Fabiana Maria Coimbra de; Carneiro, Marcella Araújo do Amaral; Uchôa, Adriana Ferreira; Santos, Elizeu Antunes dos; Morais, Ana Heloneida de Araújo
    Ingestion of peanuts may have a beneficial effect on weight control, possibly due to the satietogenic action of trypsin inhibitors. The aim of this study was to isolate a new trypsin inhibitor in a typical Brazilian peanut sweet (pac¸oca) and evaluate its effect in biochemical parameters, weight gain and food intake in male Wistar rats. The trypsin inhibitor in peanut pac¸oca (AHTI) was isolated. Experimental diets were prepared with AIN-93G supplemented with AHTI. Animals had their weight and food intake monitored. Animals were anesthetized, euthanized, and their bloods collected by cardiac puncture for dosage of cholecystokinin (CCK) and other biochemical parameters. Supplementation with AHTI significantly decreased fasting glucose, body weight gain, and food intake. These effects may be attributed to increased satiety, once supplemented animals showed no evidence of impaired nutritional status and also because AHTI increased CCK production. Thus, our results indicate that AHTI, besides reducing fasting glucose, can reduce weight gain via food intake reduction
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