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Aspergillus niger - 245, a strain isolated from soil samples showed good &#946;-fructosidase activity when inoculated in medium formulated with dahlia extract tubers. The enzyme was purified by precipitation in ammonium sulphate and percolated in DEAE-Sephadex A-50 and CM-cellulose columns, witch showed a single peack in all the purification steps, maintaining the I/S ratio between 0.32 to, 0.39. Optimum pH for inulinase activity (I) was between 4.0 - 4.5 and for invertase activity (S) between 2.5 and 5.0. The optimum temperature was 60O.C for both activities and no loss in activity was observed when it was maintained at this temperature for 30 min. The Km value was 1.44 and 5.0, respectively, for I and S and Vm value 10.48 and 30.55, respectively. The I activity was strongly inhibited by Hg2+ and Ag+ and 2 x 10-3 M of glucose, but not by fructose at the same concentration. The enzyme showed an exo-action mechanism, acting on the inulin of different origins. In assay conditions total hydrolysis of all the frutans was obtained, although it has shown larger activity on the chicory inulin than that one from artichoke Jerusalem and dahlia, in the first 30 min. The obtained results suggested that the enzyme presented good potential for industrial application in the preparing the fructose syrups Aspergillus niger - 245, isolado do solo mostrou boa atividade de b-frutosidase meio formulado com extrato de tubérculos de dahlia. A enzima foi purificada por precipitação em sulfato de amônia e percolada em colunas de DEAE-Sephadex A-50 e CM-celulose, produzindo um único pico em todas as fases de purificação e mantendo a relação I/S entre 0,32 a 0,39. O pH ótimo para a atividade de inulinase (I) foi encontrado entre 4,0 - 4.5 e para a atividade de invertase (S) em 2,5 e 5,0. A temperatura ótima foi de 60O.C para ambas as atividades e nenhuma perda foi observada quando mantida nesta temperatura por 30 min. Os valores de Km foram de 1,44 e 5,0, respectivamente, para I e S e os valores de Vm de 10,48 e 30,55, respectivamente. A atividade I foi fortemente inibida por Hg2+, Ag+ e 2 x 10-3 M de glicose, mas não por frutose na mesma concentração. A enzima mostrou um mecanismo de exo-ação, atuando sobre a inulina de diferentes origens. Em condições de ensaio foi obtida hidrólise total de frutanas, apesar de ter mostrado maior atividade sobre a inulina de chicória que sobre as de alcachofra de Jesrusalém e dahlia, nos primeiros 30 minutos de reação. Os resultados obtidos sugerem que a enzima apresenta bom potencial para aplicações industriais na preparação de xaropes de frutose

Purification and characterization of β-Fructosidase with inulinase activity from Aspergillus niger - 245