Characterization and High-level Production of D-Amino Acid Oxidase in Candida boidinii
Authors:
- 1 January 2001
- journal article
- Published by Oxford University Press (OUP) in Bioscience, Biotechnology, and Biochemistry
- Vol. 65 (3) , 627-633
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 (aod1Δ) 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 aod1Δ strain. Finally, an aod1Δ strain transformant having multi-copies of an expression plasmid on its chromosome could produce DAO amounting up to 30% of the total soluble proteins.Keywords
This publication has 26 references indexed in Scilit:
- Physiological role of theD-amino acid oxidase gene,DAO1, in carbon and nitrogen metabolism in the methylotrophic yeastCandida boidiniiYeast, 2000
- Engineering the D-amino acid oxidase from Trigonopsis variabilis to facilitate its overproduction in Escherichia coli and its downstream processing by tailor-made metal chelate supportsEnzyme and Microbial Technology, 1999
- Biotechnological application of cellular functions of the methylotrophic yeastJournal of Molecular Catalysis B: Enzymatic, 1999
- Overexpression inEscherichia coliof a Recombinant ChimericRhodotorula gracilisd-Amino Acid OxidaseProtein Expression and Purification, 1998
- The coimmobilization of d-amino acid oxidase and catalase enables the quantitative transformation of d-amino acids (d-phenylalanine) into α-keto acids (phenylpyruvic acid)Enzyme and Microbial Technology, 1998
- Molecular cloning ofTvDAO1, a gene encoding aD-amino acid oxidase fromTrigonopsis variabilis and its expression inSaccharomyces cerevisiae andKluyveromyces lactisYeast, 1997
- Immobilization of d-amino acid oxidase from different yeasts: Characterization and application in the deamination of cephalosporin CEnzyme and Microbial Technology, 1995
- Porcine D-amino acid oxidase: Production of the biologically active enzyme in Escherichia coliBiochemical and Biophysical Research Communications, 1989
- Immobilized D-Amino Acid Oxidase Preparation, Some Enzymatic Properties, and Potential UsesAgricultural and Biological Chemistry, 1974
- Demonstration of Imino Acids as Products of the Reactions Catalyzed by D- and L-Amino Acid OxidasesProceedings of the National Academy of Sciences, 1971