title: An enzymatic route to L-ornithine from L-arginine--activation and stabilization studies on L-arginase.
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.
authors.affiliation: DEGUSSA AG, Organic and Biological Chemistry Research (FCO), Hanau, Germany.
authors.forename: A S
authors.initials: AS
authors.lastname: Bommarius
authors.forename: K
authors.initials: K
authors.lastname: Makryaleas
authors.forename: K
authors.initials: K
authors.lastname: Drauz
mesh_terms: D001119:Arginase / Q000737:chemistry*; D001120:Arginine / Q000737:chemistry*; D001709:Biotechnology; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D009952:Ornithine / Q000138:chemical synthesis* / Q000737:chemistry; D013696:Temperature
chemical_list: D001120:Arginine; D009952:Ornithine; D001119:Arginase