Navegando por Autor "Pereira, Railene"

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Activity toward bruchid pest of a kunitz-type inhibitor from seeds of the algaroba tree (prosopis juliflora D.C.)
(Pesticide Biochemistry and Physiology, 2002) Morais, Ana Heloneida de Araújo; Oliveira, Adeliana; Pereira, Railene; Lima, Liziane; Franco, Octávio Luiz; Bloch Júnior, Carlos; Sá, Maria Fátima Grossi de; Sales, Maurício
A proteinaceous inhibitor with high activity against papain was found in seeds of the xerophytic algaroba tree (Prosopis julifora). The proteinase inhibitor Pj was purified using Sephacryl S-200 gel filtration followed by reverse-phase high-performance liquid chromatography on a Vidac 18 TP. Inhibitor Pj showed a Mr of 20,000 on sodium dodecyl sulfate–polyacrylamide gel electrophoresis and a Mr of 19.2K by mass spectrometry. The inhibition of papain by the Pj inhibitor was the noncompetitive type, with a Ki value of 0.59 3 1029 M. The gelatinase activity of papain was strongly inhibited by Pj too. The N-terminal amino acid sequence of the Pj inhibitor showed homology with the N-terminal amino acid sequence of the Kunitzproteinase inhibitor family. Pj was strongly effective against digestive proteinases from bean weevil Acanthoscelides obtectus and cowpea weevil Callosobruchus maculatus and was moderately active toward midgut proteinases from pod weevil Mimosestes mimosae and Mexican bean weevil Zabrotes subfasciatus. The data shown here suggest that the protein present in algaroba seeds is involved with defense responses to insects and may be an important tool to be used in engineering plants resistant to bean weevil
Analysis of an alternative food, soy paçoca, preparation: chemical composition, anti-nutricional constituents and nutricional evaluation
(Journal of Food Technology, 2003) Morais, Ana Heloneida de Araújo; Cruz, Ana; Pereira, Railene; Leite, Edda; Lima, Dilma; Sales, Maurício Pereira de
The chemical composition of an alternative Brazilian food preparation showed that this product had a carbohydrate content of 45.90% and a protein content of 38.92%. Anti-nutritional factors were assayed in soya "pacoca" protein fractions. Human salivary alpha -amylase was inhibited with salivary amylase inhibitor ( alpha -IA) level of 437.5 micro g of inhibitor to 1.0 mg of protein fractions. Trypsin was inhibited with trypsin inhibitor activities level (TIA) of 57 micro g of inhibitor to 1.0 g of protein fractions. Nutritional evaluation of the soya "pacoca" showed a digestibility of 66.9% compared to 90.0% for casein. The PER of soya "pacoca" was 1.65 and was 4.01 for casein. The NPR of the food preparation was 2.85 and the test diet was 3.02. Indices calculated for the soya "pacoca" food preparation indicated that it was less efficient in supporting growth and maintenance of the weanling rats
Comparative digestibility and the inhibition of mammalian digestive enzymes from mature and immature cowpea (Vigna unguiculata (L.) Walp.) seeds
(Food Control, 2004) Morais, Ana Heloneida de Araújo; Lima, Liziane Maria de; Oliveira, Antônia Elenir Amâncio; Pereira, Railene; Miranda, Maria Raquel Alcântara de; Sales, Maurício Pereira de
Globulins and albumins from mature cowpea seeds had inhibitory activity levels of 9.5 and 67.1 units trypsin inhibited per mg protein and globulins and albumins from immature seeds had trypsin inhibitory activity levels of 6.3 and 26.6 units trypsin inhibited per mg protein, respectively. Albumins from immature seeds had inhibitory activity level of 4 units salivary amylase inhibited per mg albumin. The globulins (native and heated) from both seeds were submitted to hydrolysis by trypsin and analyzed by SDS-PAGE. Native globulins from mature and immature seeds showed digestion products of ∼30 and ∼20 kDa, respectively. Trypsin strongly digested heated globulins from both kinds cowpeas
In vitro digestibility of globulins from cowpea (vigna unguiculata) and xerophitic algaroba (prosopis juliflora) seeds by mammalian digestive proteinases: a comparative study
(Food Chemistry, 2002) Morais, Ana Heloneida de Araújo; Oliveira, Adeliana; Lima, Liziane; Pereira, Railene; Cardoso, Patrícia; Miranda, Maria Raquel; Sales, Maurício; Xavier Filho, José
Globulins were purified from mature and immature cowpea and algaroba seeds by gel filtration (S-200), anion exchange (DEAE-Sepharose) and other chromatographic methods. These globulins (native and heated) were submitted to hydrolysis by pepsin, chymotrypsin and trypsin and their digestion products were analysed by SDS-PAGE. Results showed that native globulins of both legumes were weakly digested by pepsin and were not digested by serine proteases. Heated proteins from cowpea were digested more rapidly by pepsin and chymotrypsin than was algaroba globulin. Trypsin rapidly digested proteins from both cowpea and algaroba. Comparing the hydrolysis of bean globulins to the algaroba globulins by mammalian enzymes, the globulins from immature cowpea showed better digestibility than mature cowpea; globulins from algaroba pod, which is used as an alternative food, were difficult to digest

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Navegando por Autor "Pereira, Railene"