Open AccessTrigonopsis variabilisd -Amino Acid Oxidase: Control of Protein Quality and Opportunities for Biocatalysis through Production inEscherichia coli
Author(s) -
Iskandar Dib,
Damir Stanzer,
Bernd Nidetzky
Publication year - 2007
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.01569-06
Subject(s) - escherichia coli , d amino acid oxidase , food science , biocatalysis , biochemistry , chemistry , oxidase test , enzyme , biology , microbiology and biotechnology , gene , ionic liquid , catalysis
Trigonopsis variabilis d -amino acid oxidase accounts for 35% ofEscherichia coli protein when addedd -methionine suppresses the toxic activity of the recombinant product. PermeabilizedE. 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.