Enhanced metalloadsorption of bacterial cells displaying poly-His peptides

Journal Article · Thu Aug 01 04:00:00 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, Journal Name: Bio/Technology Journal Issue: 8 Vol. 14; ISSN 0733-222X; ISSN BTCHDA
• Country of Publication: United States
• Language: English

Related Subjects

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