Anais do Simpósio Nacional de Bioprocessos
XXII National Bioprocesses Symposium (SINAFERM) XIII Enzymatic Hydrolysis of Biomass Symposium (SHEB)

L-asparaginases are applied in fried potatos, bread and biscuits to reduce acrylamide formation. The present study aimed at the purification and characterization of L-asparaginase from Aspergillus oryzae IOC 3999. The L-asparaginase was purified 2.1 fold by 30 KDa membrane ultrafiltration and Sephadex G 100 column chromatography. The purified enzyme exhibited optimum activity at pH 5 and at 60 °C. The L-asparaginase showed stability at 50 °C for 1 h and in the range of pH 4 to 7 during 1 h at 10 °C. The L-asparaginase presented values of Km and Vmax equal to 5.22 mM and 52.91 (U/mL), respectively for the substrate L-asparagine.