Record Display for the EPA National Library Catalog


Main Title Exploitation of the High Affinity and Specificity of Proteins in Waste Stream Treatment.
Author Furlong, C. E. ; Sundstrom, J. A. ; Weiler, E. B. ; Cheung, P. W. ; Yin, J. ;
CORP Author Washington Univ., Seattle. ;California Univ., Berkeley. Dept. of Chemical Engineering.;Environmental Protection Agency, Cincinnati, OH. Risk Reduction Engineering Lab.
Publisher c1988
Year Published 1988
Report Number EPA/600/D-88/229;
Stock Number PB89-118442
Additional Subjects Phosphates ; Proteins ; Waste treatment ; Water pollution control ; Cadmium ; Escherichia coli ; Peptides ; Scrubbers ; Reprints ; Metallothionein ; Carrier proteins ; Bacterial proteins ; Bioreactions
Library Call Number Additional Info Location Last
NTIS  PB89-118442 Some EPA libraries have a fiche copy filed under the call number shown. 07/26/2022
Collation 12p
The purpose of the research was to test the feasibility of using immobilized proteins as highly specific adsorbers of pollutants in waste streams. The Escherichia coli periplasmic phosphate-binding protein served as both a model system for determining the feasibility of such an approach and at the same time was used to produce a cycling ligand adsorber capable of efficiently scrubbing phosphate from a feed stream. Three different procedures for the removal of cadmium from feed streams were developed. One involved an immobilized metallothionein (a natural mammalian protein). The second involved use of an immobilized plant peptide, and the third involved the synthesis of a resin that mimics the backbone structure of the naturally occurring plant peptides. A bioreactor for continuous protein production was developed to minimize the cost of protein production. The bioreactor contained immobilized, non-growing E. coli cells. The cell line had been mutagenized and selected for the direct secretion of periplasmic proteins into the medium. The cells contained the gene that encodes the phosphate-binding protein.