Isolamento, fracionamento e caracterização parcial das proteínas de amêndoa de Baru (Dipteryx alata Vog.)
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2010-11-09
Autores
Cruz, Kézia Soares da [UNESP]
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Universidade Estadual Paulista (Unesp)
Resumo
O baru (Dipteryx alata Vog.), fruta nativa do Cerrado brasileiro, apresenta uma amêndoa com alto teor de proteínas, entretanto, informações sobre suas propriedades são ainda escassas. O objetivo do trabalho foi caracterizar algumas das propriedades físico-químicas da proteína dessa semente. Percentuais de 74,13; 81,56 e 76,50 de proteínas foram solubilizadas frente às diferentes proporções massa:volume 1:10, 1:30 e 1:50, respectivamente. Em relação aos tempos 30, 60 e 90 minutos de extração solubilizaram-se 78,59, 80,45 e 73,74% das proteínas totais, respectivamente. Frente às modificações de pH e concentração de NaCl, verificouse um comportamento típico da predominância de globulinas, caracterizado por máxima solubilidade em pHs 2,0 (87,9%) e acima de 8,0 (89,87%) e mínima solubilidade (8,5%) em pH 4,5, em água, e aumento junto ao ponto isoelétrico associado a crescente concentração salina no meio extrator. O fracionamento pelo critério de solubilidade em diferentes sistemas revelou teores de 13,97% de albuminas; 61,74% de globulinas, 0,48% de prolaminas, 3,25% de glutelinas e 4,61% de proteínas insolúveis. A digestibilidade in vitro, determinada pela sequência enzimática pepsina-pancreatina, mostrou 85,59% e 90,54% de hidrólise em relação à caseína para a farinha desengordurada e a globulina total da amêndoa, respectivamente. A proteólise da globulina majoritária obtida em Sephadex G-200, pelas enzimas tripisina, quimotripsina e pepsina, separadamente, mostrou percentuais de hidrólise, em relação à caseína, de 62,38, 17,92 e 71,38, respectivamente, após 120 minutos de incubação, sendo o progresso das proteólises acompanhados em SDS-PAGE. O perfil cromatográfico em colunas de filtração em gel mostrou a existência de uma forma protéica majoritária na fração globulina total que, em coluna de troca-iônica de DEAE-celulose, foi eluída...
The Baru (Dipteryx alata Vog.), a fruit native to the Brazilian Cerrado, has a seed with a high protein content, however, informations about its properties remain scarce. The aim of this study was to characterize some of the physicochemical properties of this seed protein. Protein percentage of 74.13, 81.56 and 76.50 were solubilized using the mass:volume ratios 1:10, 1:30 and 1:50, respectively. During the extraction times 30, 60 and 90 minutes were solubilized 78.59, 80.45 and 73.74% of total proteins, respectively. Changes in pH and salt concentration reveled a typical behavior of gobulin predominance, characterized by greater solubility at pH 2.0 (87.9%) and above 8.0 (89.87%) and lower solubility (8.5%) at pH 4.5 in water, and solubility improvement near the isoelectric pH by increasing salt concentration in the extractant. Fractionation according to protein solubility in different solvents showed 13.97, 61.74, 0.48, 3.25 and 4.61 percent of albumin, globulin, prolamin, glutelin and insoluble protein, respectively. The in vitro digestibility determined by pepsin-pancreatin enzimatic sequence showed 85.59% and 90.54% of hydrolysis, in relation to casein, for the defatted flour and total globulin from baru seed, respectively. After 120 minutes of incubation, proteolysis of the major globulin obtained from Sephadex G-200 by tripsin, chymotrypsin and pepsin, separately, showed hydrolysis porcentages, in relation to casein, of 62.38, 17.92 and 71.38, respectively, and the progress of these proteolysis was monitored by SDS-PAGE. The chromatographic profile in gel filtration columns reveled the existence of one major protein form in total globulin, which was eluted off the DEAE-celulose ionexchange column at 0.12 M NaCl concentration. The molecular weight (MW) of globulin was estimated at 405-436 kDa and its electrophoretic profile showed three main bands of MW 62-64, 66 and 73-76 kDa, and... (Complete abstract click electronic access below)
The Baru (Dipteryx alata Vog.), a fruit native to the Brazilian Cerrado, has a seed with a high protein content, however, informations about its properties remain scarce. The aim of this study was to characterize some of the physicochemical properties of this seed protein. Protein percentage of 74.13, 81.56 and 76.50 were solubilized using the mass:volume ratios 1:10, 1:30 and 1:50, respectively. During the extraction times 30, 60 and 90 minutes were solubilized 78.59, 80.45 and 73.74% of total proteins, respectively. Changes in pH and salt concentration reveled a typical behavior of gobulin predominance, characterized by greater solubility at pH 2.0 (87.9%) and above 8.0 (89.87%) and lower solubility (8.5%) at pH 4.5 in water, and solubility improvement near the isoelectric pH by increasing salt concentration in the extractant. Fractionation according to protein solubility in different solvents showed 13.97, 61.74, 0.48, 3.25 and 4.61 percent of albumin, globulin, prolamin, glutelin and insoluble protein, respectively. The in vitro digestibility determined by pepsin-pancreatin enzimatic sequence showed 85.59% and 90.54% of hydrolysis, in relation to casein, for the defatted flour and total globulin from baru seed, respectively. After 120 minutes of incubation, proteolysis of the major globulin obtained from Sephadex G-200 by tripsin, chymotrypsin and pepsin, separately, showed hydrolysis porcentages, in relation to casein, of 62.38, 17.92 and 71.38, respectively, and the progress of these proteolysis was monitored by SDS-PAGE. The chromatographic profile in gel filtration columns reveled the existence of one major protein form in total globulin, which was eluted off the DEAE-celulose ionexchange column at 0.12 M NaCl concentration. The molecular weight (MW) of globulin was estimated at 405-436 kDa and its electrophoretic profile showed three main bands of MW 62-64, 66 and 73-76 kDa, and... (Complete abstract click electronic access below)
Descrição
Palavras-chave
Proteínas, Diperyx alata, Fracionamento, Digestibilidade in vintro, Dipteryx alata Vog, Baru, Proteins, Fractionation, In vitro digestibility
Como citar
CRUZ, Kézia Soares da. Isolamento, fracionamento e caracterização parcial das proteínas de amêndoa de Baru (Dipteryx alata Vog.). 2010. 103 f. Dissertação (mestrado) - Universidade Estadual Paulista, Faculdade de Ciências Farmacêuticas, 2010.