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Enzymatic Synthesis of Agmatine by Immobilized Escherichia coli Cells with Arginine Decarboxylase Activity 被引量:3

Enzymatic Synthesis of Agmatine by Immobilized Escherichia coli Cells with Arginine Decarboxylase Activity
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摘要 A new method for the enzymatic synthesis of agmatine by immobilized Escherichia coli cells with arginine decarboxylase(ADC) activity was established and a series of optimal reaction conditions was set down. The arginine 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 substrate concentration was 100 mmol/L and the reaction time was 15 h. It was also observed that the appropriate concentration of Mg2+, especially at 0.5 mmol/L promoted the arginine decarboxylase activity; Mn2+ had little effect on the arginine decarboxylase activity. The inhibition of Cu2+ and Zn2+ to the arginine decarboxylase activity was significant. 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 agmatine, leaving the pure optically D-arginine simultaneously. The method has a very important guiding significance to the enzymatic preparation of agmatine. A new method for the enzymatic synthesis of agmatine by immobilized Escherichia coli cells with arginine decarboxylase(ADC) activity was established and a series of optimal reaction conditions was set down. The arginine 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 substrate concentration was 100 mmol/L and the reaction time was 15 h. It was also observed that the appropriate concentration of Mg2+, especially at 0.5 mmol/L promoted the arginine decarboxylase activity; Mn2+ had little effect on the arginine decarboxylase activity. The inhibition of Cu2+ and Zn2+ to the arginine decarboxylase activity was significant. 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 agmatine, leaving the pure optically D-arginine simultaneously. The method has a very important guiding significance to the enzymatic preparation of agmatine.
出处 《Chemical Research in Chinese Universities》 SCIE CAS CSCD 2011年第6期992-995,共4页 高等学校化学研究(英文版)
基金 Supported by the National Technology-Innovation Fund of China(No.02CJ-13-01-16)
关键词 Arginine decarboxylase AGMATINE Enzymatic resolution Immobilized cell Arginine decarboxylase Agmatine Enzymatic resolution Immobilized cell
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