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  • Title: An enzymatic route to L-ornithine from L-arginine--activation and stabilization studies on L-arginase.
    Author: Bommarius AS, Makryaleas K, Drauz K.
    Journal: Biomed Biochim Acta; 1991; 50(10-11):S249-55. PubMed ID: 1820054.
    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.
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