Enhanced metalloadsorption of bacterial cells displaying poly-His peptides

Journal Article · Thu Aug 01 00:00:00 EDT 1996 · Bio/Technology

DOI:https://doi.org/10.1038/nbt0896-1017· OSTI ID:508323

Sousa, C; Cebolla, A; Lorenzo, V de ^[1]

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1. CSIC, Madrid (Spain)

The properties of Escherichia coli cells, acquired by cell surface presentation of one or two hexahistidine (His) clusters carried by the outer membrane LamB protein, have been examined. Strains producing LamB hybrids with the His chains accumulated greater than 11-fold more Cd{sup 2} than E. coli cells expressing the protein without the His insert. Furthermore, the hexa-His chains on the cell surface caused cells to adhere reversibly to a Ni{sup 2+}-containing solid matrix in a metal-dependent fashion. Thus, expression of poly-His peptides enables bacteria to act as a metalloaffinity adsorbent. These results open up the possibility for biosorption of heavy ions using engineered microorganisms. 32 refs., 3 figs.

• OSTI ID: 508323
• Journal Information: Bio/Technology, Vol. 14, Issue 8; Other Information: PBD: Aug 1996
• Country of Publication: United States
• Language: English

Related Subjects

54 ENVIRONMENTAL SCIENCES
55 BIOLOGY AND MEDICINE
BASIC STUDIES
BIOADSORBENTS
EVALUATION
HEAVY IONS
ADSORPTION
QUANTITATIVE CHEMICAL ANALYSIS
CADMIUM
BIOLOGICAL ACCUMULATION
NICKEL
LIQUID WASTES
REMEDIAL ACTION
DECONTAMINATION
PROTEINS
HYBRIDIZATION
GENES
GENE REGULATION
STRUCTURE-ACTIVITY RELATIONSHIPS
BACTERIA
PEPTIDES
HISTIDINE
AMINO ACIDS
ESCHERICHIA COLI
ANIMAL CELLS
PLASMIDS
ABSORPTION SPECTROSCOPY