著者
Kadoya Ryosuke Matsumoto Ken'ichiro Ooi Toshihiko Taguchi Seiichi
出版者
PLOS
雑誌
PLOS one (ISSN:19326203)
巻号頁・発行日
vol.10, no.6, 2015-06-04
被引用文献数
19

Bacterial polyester polyhydroxyalkanoates (PHAs) have been produced in engineered Escherichia coli, which turned into an efficient and versatile platform by applying metabolic and enzyme engineering approaches. The present study aimed at drawing out the latent potential of this organism using genome-wide mutagenesis. To meet this goal, a transposon-based mutagenesis was carried out on E. coli, which was transformed to produce poly (lactate-co-3-hydroxybutyrate) from glucose. A high-throughput screening of polymer-accumulating cells on Nile red-containing plates isolated one mutant that produced 1.8-fold higher quantity of polymer without severe disadvantages in the cell growth and monomer composition of the polymer. The transposon was inserted into the locus within the gene encoding MtgA that takes part, as a non-lethal component, in the formation of the peptidoglycan backbone. Accordingly, the mtgA-deleted strain E. coli JW3175, which was a derivate of superior PHA-producing strain BW25113, was examined for polymer production, and exhibited an enhanced accumulation of the polymer (7.0 g/l) compared to the control (5.2 g/l). Interestingly, an enlargement in cell width associated with polymer accumulation was observed in this strain, resulting in a 1.6-fold greater polymer accumulation per cell compared to the control. This result suggests that the increase in volumetric capacity for accumulating intracellular material contributed to the enhanced polymer production. The mtgA deletion should be combined with conventional engineering approaches, and thus, is a promising strategy for improved production of intracellularly accumulated biopolymers.
著者
TAGUCHI SEIICHI ARAKAWA KUMIKO YOKOYAMA KEIICHI TAKEHANA SHINO TAKAGI HIROSHI MOMOSE HARUO
出版者
The Society for Biotechnology, Japan
雑誌
Journal of Bioscience and Bioengineering (ISSN:13891723)
巻号頁・発行日
vol.94, no.5, pp.478-481, 2002
被引用文献数
1

Processing and activation of the precursor of an extracellular <i>Streptomyces</i> transglutaminase were achieved by using three <i>Streptomyces</i> proteases (SAM-P20, SAM-P26 and SAM-P45), all of which are widely distributed in <i>Streptomyces</i>. The use of these proteases would allow us to develop a production process for the active form of this enzyme in recombinant bacteria.<br>