Abstract
The paper presents the results of studies to determine the optimal functioning parameters of aspartase and fumarase of the bacterial strain P. carotovorum MDC-8727, an aspartase producer. The temperature and pH optima of both enzymes are close and are in the range of T (35-40 °C) and pH (8.5-9.0). At a temperature of 50 °C, the thermal stability of aspartase is twice higher than that of fumarase. It was found that thermal treatment of cell biomass in the culture broth at low pH values contributed to the partial inactivation of fumarase. A similar treatment of cells at temperature of 50 °C and pH 5 for 90 minutes contributed to the complete inactivation of fumarase without harming the aspartase activity. fumarase, aspartase, L-aspartic acid, biotransformation
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