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An enzymatic route to L-ornithine from L-arginine--activation and stabilization studies on L-arginase.

Bommarius As, Kyriakos Makryaleas, Karlheinz Drauz

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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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What this paper is about

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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Available 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.

Key concepts: Arginase, Ornithine, Chemistry, Arginine, Enzyme, Ascorbic acid, Biochemistry, Amino acid

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An enzymatic route to L-ornithine from L-arginine--activation and stabilization studies on L-arginase. — Research Paper | ScholarLens