Bacterium-based heavy metal biosorbents: enhanced uptake of cadmium by E. coli expressing a metallothionein fused to beta-galactosidase.
We investigated the potential utility of a recombinant E. coli that expresses the human metallothionein II gene as a fusion protein with beta-galactosidase as a heavy metal biosorbent. E. coli cells expressing the metallothionein fusion demonstrated enhanced binding of Cd2+ compared to cells that lack the metallothionein. It was shown that the metallothionein fusion was capable of efficiently removing Cd2+ from solutions. Approximately 40% of the Cd2+ accumulated by the recombinant cells free in suspension was associated with the outer cell membrane, and 60% of that was present in the cytoplasm.
Yoshida
N
N
Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, Miyazaki University, Japan. a04109u@cc.miyazaki-u.ac.jp
Kato
T
T
Yoshida
T
T
Ogawa
K
K
Yamashita
M
M
Murooka
Y
Y
D001673:Biodegradation, Environmental; D002104:Cadmium / Q000493:pharmacokinetics*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D015964:Gene Expression Regulation, Bacterial; D008668:Metallothionein / Q000235:genetics*; D008854:Microscopy, Electron; D011993:Recombinant Fusion Proteins / Q000235:genetics; D001616:beta-Galactosidase / Q000235:genetics*
D011993:Recombinant Fusion Proteins; D002104:Cadmium; D008668:Metallothionein; D001616:beta-Galactosidase