Trigonopsis variabilis D-amino acid oxidase: control of protein quality and opportunities for biocatalysis through production in Escherichia coli.
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ABSTRACT:
SUBMITTER: Dib I
PROVIDER: S-EPMC1797113 | biostudies-literature | 2007 Jan
REPOSITORIES: biostudies-literature
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Trigonopsis variabilis D-amino acid oxidase: control of protein quality and opportunities for biocatalysis through production in Escherichia coli.
Dib Iskandar I Stanzer Damir D Nidetzky Bernd B
Applied and environmental microbiology 20061020 1
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. ...[more]
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