Enzymatic Synthesis of Agmatine by Immobilized Escherichia coli Cells with Arginine Decarboxylase Activity

A new method for the enzymatic synthesis of agmatine by immobilized Escherichia coli cells with argi- nine decarboxylase(ADC) activity was established and a series of optimal reaction conditions was set down. The ar- ginine decarboxylase showed the maximum activity when the pyridoxal phosphate(PLP) concentration was 50 mmol/L, pH=7 and 45 °C. The arginine decarboxylase exhibited the maximum production efficiency when the sub- strate concentration was 100 mmol/L and the reaction time was 15 h. It was also observed that the appropriate con- centration of Mg 2+ , especially at 0.5 mmol/L promoted the arginine decarboxylase activity; Mn 2+ had little effect on the arginine decarboxylase activity. The inhibition of Cu 2+ and Zn 2+ to the arginine decarboxylase activity was sig- nificant. The immobilized cells were continuously used 6 times and the average conversion rate during the six-time usage was 55.6%. The immobilized cells exhibited favourable operational stability. After optimization, the maximally cumulative amount of agmatine could be up to 20 g/L. In addition, this method can also catalyze D,L-arginine to ag- matine, leaving the pure optically D-arginine simultaneously. The method has a very important guiding significance to the enzymatic preparation of agmatine. Keywords Arginine decarboxylase; Agmatine; Enzymatic resolution; Immobilized cell Article ID 1005-9040(2011)-06-992-04