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O objetivo deste trabalho foi determinar as melhores condições de hidrólise enzimática de fibras alimentares de cotilédones de soja, original (FAO) e micronizada (FAM), e caracterizar os hidrolisados sólidos e solúveis. As amostras foram hidrolisadas com carboidrase (200 µL g-1, durante 12 horas, a 30ºC) ou com protease (150 µL g-1, durante 5 horas, a 55ºC). A fração sólida das amostras tratadas com carboidrase teve redução de 73% dos carboidratos e de 50% dos ácidos urônicos iniciais; houve aumento da concentração de proteínas e aumento da solubilidade e volume de intumescimento comparado com o material não hidrolisado. Proteínas de reserva da soja - beta-conglicinina e glicinina - foram extraídas das fibras alimentares não hidrolisadas e identificadas por eletroforese. A protease solubilizou 54% do total de proteínas das amostras e formou peptídeos com peso molecular menor que 10 KDa e uma banda de peso molecular próximo aos 25 KDa, provavelmente glicoproteína de parede celular, e deixou uma fração sólida com 76% de fibras alimentares totais. A microscopia eletrônica de varredura mostrou alterações físicas para a FAO hidrolisada com protease, com superfície mais porosa do que a FAM. O tratamento enzimático foi efetivo em alterar a composição química e estrutural das fibras, dando novas perspectivas para aplicações tecnológicas. The objective of this work was to determine the best enzymatic hydrolysis conditions for dietary fiber from soybean cotyledons, original (ODF) and milled (MDF), and to characterize the solid and soluble hydrolytes. The samples were hydrolyzed with carbohydrase (200 µL g-1 for 12 hours, at 30ºC) or protease (150 µL g-1 for 5 hours, at 55ºC). The solid fraction of the samples treated with carbohydrase had a reduction of 73% for the carbohydrates and of 50% for the uronic acids of the initial material; there was an increase in protein concentration and in solubility and swelling volume in comparison to the nonhydrolyzed material. Soybean storage proteins - beta-conglycinin and glycinin - were extracted from nonhydrolyzed dietary fiber and identified by electrophoresis. Protease solubilized 54% of the sample's total protein content, formed peptides with molecular weight lower than 10 KDa, a band with molecular weight of 25 KDa probably cell-wall glycoprotein, and left a solid fraction with 76% total dietary fiber. Scanning electron microscopy showed physical alterations for ODF hydrolyzed with protease, with more superficial pores than MDF. The enzymatic treatment was effective in altering the chemical and structural composition of the fibers, resulting in new perspectives for technological applications

Hidrólise enzimática de fibras de cotilédones de soja e caracterização das frações sólidas e solúveis