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149 results about "Arginase" patented technology

Arginase (EC 3.5.3.1, arginine amidinase, canavanase, L-arginase, arginine transamidinase) is a manganese-containing enzyme. The reaction catalyzed by this enzyme is: arginine + H₂O → ornithine + urea. It is the final enzyme of the urea cycle. It is ubiquitous to all domains of life.

Protection against herbivores

The present invention relates to genes, proteins and methods comprising molecules that alter amino acid levels. In one embodiment, the present invention relates to altering guanidino substrate hydrolysis activities in plants, arthropods and microorganisms using molecules within the arginase family and other molecules that alter an amino acid levels. In ones embodiment, the present invention relates to altering threonine substrate deamination and dehydration activities in plants, arthropods and microorganisms using molecules within the threonine deaminase family and other molecules that alter amino acid levels. In one embodiment, the present invention relates to using genes, proteins and methods comprising arginase or threonine deaminase for altering the pathophysiology of plants, arthropods and microorganisms. In a preferred embodiment, the present invention relates to altering guanidino substrate hydrolysis activity in plants, arthropods, and microorganisms using arginase. In another preferred embodiment, the invention relates to altering threonine substrated deamination and dehydration activity in plants, arthropods, and microorganisms using threonine deaminase. In some embodiments, the invention related to overexpression and increased activity of arginase, threonine deaminase and a proteinase inhibitor.
Owner:BOARD OF TRUSTEES OPERATING MICHIGAN STATE UNIV

Method for immobilizing human source arginase-1 through surface display

The invention discloses a method for immobilizing human source arginase-1 through surface display. The method comprises the steps of adding signal peptide and charged polypeptide to the amino terminal of a protein cleavage variant (InaK-N) formed on an ice core, fusing human source arginase-1 into the carboxyl terminal, and designing an HA label at the carboxyl terminal; constructing various recombinant plasmids to convert competent escherichia coli cells, so that different genetic engineering strains are obtained; conducting shake-flask culture on the strains; detecting the display efficiency and enzyme activity of human source arginase-1; selecting the strain with the highest enzyme activity for mass culture, conducting efficient L-arginine conversion, and synthesizing L-ornithine. Human source arginase-1 fused in the protein cleavage variant formed on the ice core is effectively displayed on the surface of an escherichia coli cell, so that human source arginase-1 is immobilized. Compared with an original ice core protein display system, the method has the advantage that the display efficiency and enzyme activity of human source arginase-1 are improved remarkably. Compared with a chitin immobilizing method, the method has the advantages that cost is reduced, process is shortened, and purification steps are simplified.
Owner:HUBEI UNIV
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