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An enzymatic route to L-ornithine from L-arginine--activation and stabilization studies on L-arginase
A S Bommarius1, K Makryaleas, K Drauz
1DEGUSSA AG, Organic and Biological Chemistry Research (FCO), Hanau, Germany.
Abstract:
L-ornithine has growth potential for parenteral nutrition and as a component for biologically active peptides. A process for enzymatic conversion of L-arginine to L-ornithine with arginase has been developed and tested on a pilot scale. With activation of arginase by Mn2+ and stabilization by ascorbic acid, the enzyme is sufficiently active and stable for application in large-scale L-ornithine synthesis.