L-lysine α-oxidase
(LO) is one of a few microbial enzymes with therapeutic potential in certain
cancers. The enzyme has been determined in several bacteria and fungi. Its
production is mainly regulated by carbon sources and oxygen. . Thus, the aim of
this study was to determine the nutritional requirements and effect of oxygen
concentration on the production of LO in P. aeruginosa, and in their
recombinants using a highly efficient oxygen uptake system, the Vitreoscilla
hemoglobin. This study concerns the effect of a higher oxygen uptake provided
by a recombinant system, the Vitreoscilla
hemoglobin, on the production of LO in Pseudomonas
aeruginosa. The results showed that
the recombinant bacterium expressing Vitreoscilla
hemoglobin gene (vgb) had distinct
L-lysine activity from the host strain under both carbon catabolite repression
and no repression conditions. In a rich medium supplemented with glucose, the
recombinant strain showed 20-40 % higher L-lysine activity than the host
strain. This difference was even more significant in the medium with no glucose
supplement, where the recombinant strain showed almost 2-fold higher enzyme
activity throughout the incubation. The results sometime were contradictory in
terms of the effect of carbon source (mainly glucose) and oxygen on the
production of this enzyme.
Vitreoscilla hemoglobin Psedomonas aeruginosa L-lysine α-oxidase
Birincil Dil | İngilizce |
---|---|
Bölüm | TJST |
Yazarlar | |
Yayımlanma Tarihi | 19 Eylül 2018 |
Gönderilme Tarihi | 8 Mart 2018 |
Yayımlandığı Sayı | Yıl 2018 Cilt: 13 Sayı: 2 |