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  • Title: Characterization and high-level production of D-amino acid oxidase in Candida boidinii.
    Author: Yurimoto H, Hasegawa T, Sakai Y, Kato N.
    Journal: Biosci Biotechnol Biochem; 2001 Mar; 65(3):627-33. PubMed ID: 11330678.
    Abstract:
    D-Amino acid oxidase (DAO, EC 1.4.3.3) from a methylotrophic yeast, Candida boidinii, was produced at a high level under the control of the alcohol oxidase gene promoter in the original host. The enzyme was a peroxisomal and monomeric enzyme, and contained noncovalently-bound FAD as a cofactor. The enzyme was active toward several D-amino acids such as D-Ala, D-Met, and D-Ser. An alcohol oxidase-depleted strain (aod1delta) was found to be a more suitable host for DAO production than the wild-type strain. Several post-translational effects may be responsible for the improvement of the DAO productivity by the aod1delta strain. Finally, an aod1delta strain transformant having multi-copies of an expression plasmid on its chromosome could produce DAO amounting up to 30% of the total soluble proteins.
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