Determinação da atividade antitríptica em proteínas de produtos do amendoim isoladas por cromatografia de afinidade

AUTOR(ES)

Araújo, Jéssica Morais de, Alves, Jussara Cristina, Peixoto, Thayane Kerbele Oliveira das Neves, Medeiros, Amanda Fernandes de, Machado, Richele Janaína de Araújo, Serquiz, Alexandre Coelho, Neves, Renata Alexandra Moreira das, Santos, Elizeu Antunes dos, Uchôa, Adriana Ferreira, Morais, Ana Heloneida de Araújo

FONTE

Quím. Nova

DATA DE PUBLICAÇÃO

2014

RESUMO

The peanut is an oleaginous plant of high nutritional value, a source of protein and a trypsin inhibitor. Trypsin inhibitors are proteins present in the vegetable kingdom, considered anti-nutritional factors for animals. However, there have been several recent reports about their heterologous and beneficial effects on human health. These important effects have been the focus of studies investigating these inhibitors in foods. The aim of the present study was to isolate and determine the estimated molecular mass and specific inhibitory activity, for trypsin in the Japanese peanut, peanut butter, and peanut nougat using the techniques of precipitation with ammonium sulfate and affinity chromatography on trypsin - Sepharose CNBr 4B. The techniques used in this study were efficient for isolating the protein inhibitors with antitryptic specific activity of 694 UI mg-1, 823 UI mg-1 and 108 UI mg-1 for the Japanese peanut, peanut nougat, and peanut butter, respectively. The techniques featured high selectivity of the adsorbent, with consequent efficiency in isolation, given the low amount of dosed proteins and specific antitryptic activity presented by the products studied. The various health-related benefits show the importance of detecting and isolating efficient trypsin inhibitors in foods, taking into account the health claims attributed to the vegetable and its high consumption by humans.

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