Article ID Journal Published Year Pages File Type
69466 Journal of Molecular Catalysis B: Enzymatic 2015 8 Pages PDF
Abstract

•A novel process was established for agmatine production using arginine decarboxylase.•High conversion rate (95.6%) was obtained.•Transformation time was just 6 h.

In this study, a novel process for enzymatic production of agmatine from l-arginine using recombinant arginine decarboxylase (ADC) was established. The speA gene encoding ADC was expressed in Escherichia coli BL21 (DE3) in a soluble and active form, and recombinant ADC exhibited a maximum specific activity of 0.53 U mg−1 following optimization of culture conditions using an orthogonal array experiment. Up to 14.3 g l−1 of agmatine was obtained from 20 g l−1 of l-arginine in 6 h under optimum conditions (3.5 g l−1 intact cells, 4 mM Mg2+, 30 mM pyridoxal-5′-phosphate (PLP), pH 7, 37 °C). This represents a significant improvement in a method for production of agmatine.

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Related Topics
Physical Sciences and Engineering Chemical Engineering Catalysis
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