Abstract
We investigated the potential utility of a recombinant E. coli that expresses the human metallothionein II gene as a fusion protein with β-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.
Original language | English |
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Pages (from-to) | 551-558 |
Number of pages | 8 |
Journal | BioTechniques |
Volume | 32 |
Issue number | 3 |
DOIs | |
Publication status | Published - 2002 |
Externally published | Yes |
ASJC Scopus subject areas
- Biotechnology
- Biochemistry, Genetics and Molecular Biology(all)