Trigonopsis variabilis D-amino acid oxidase: control of protein quality and opportunities for biocatalysis through production in Escherichia coli.
Trigonopsis variabilis D-amino acid oxidase accounts for 35% of Escherichia coli protein when added D-methionine suppresses the toxic activity of the recombinant product. Permeabilized E. coli cells are reusable and stabilized enzyme preparations. The purified oxidase lacks the microheterogeneity of the natural enzyme. Oriented immobilization of a chimeric oxidase maintains 80% of the original activity in microparticle-bound enzymes.
Dib
Iskandar
I
Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12/I, A-8010 Graz, Austria.
Stanzer
Damir
D
Nidetzky
Bernd
B
D000409:Alanine / Q000378:metabolism*; D001709:Biotechnology / Q000379:methods; D002384:Catalysis; D003470:Culture Media; D003605:D-Amino-Acid Oxidase / Q000235:genetics / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D010316:Particle Size; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism*; D004718:Saccharomycetales / Q000201:enzymology* / Q000235:genetics
D003470:Culture Media; D004800:Enzymes, Immobilized; D011994:Recombinant Proteins; D003605:D-Amino-Acid Oxidase; D000409:Alanine