This paper gives an overview of the feasibility of the application of biotechnology to nuclear waste treatment. The contents are based on a report which PA Technology carried out for the Department of the Environment (DoE Reference: DoE/RW/88.008 Sector No 2.3).
Many living and dead organisms accumulate heavy metals and radionuclides. The controlled use of this phenomenon forms the basis for the application of biotechnology to the removal of radionuclides from nuclear waste streams. Indeed, biotechnology offers a series of new opportunities for removal of radionuclides from dilute aqueous process effluents. Such technology is already used for heavy metal removal on a commercial basis and could be optimised for radionuclide removal.
An overview of biotechnology areas, namely the use of biopolymers and biosorption using biomass applicable to the removal of radionuclides from industrial nuclear effluents is given. The potential of biomagnetic separation technology, genetic engineering and monoclonal antibody technology is also to be examined. The most appropriate technologies to develop for radionuclide removal in the short term appear to be those based on biosorption of radionuclides by biomass and the use of modified and unmodified biopolymers in the medium term.
6,7-Dideoxy-D-gluco-heptonic-7-phosphonic acid, the isosteric phosphonate analogue of gluconate 6-phosphate, was prepared by incubation of the corresponding analogue of glucose 6-phosphate with glucose 6-phosphate dehydrogenase and NADP+ in the presence of an enzyme NADPH-NADP+ recycling system. The analogue of gluconate 6-phosphate is a substrate for yeast gluconate 6-phosphate dehydrogenase, showing Michaelis-Menten kinetics at pH 7.5 and 8.0. At both pH values the Km values are approx. 3-fold higher and the Vmax. values approx. 7-fold lower than those of the natural substrate.
Free ribulose bisphosphate (RuBP(4-)) rather than its magnesium complex (RuBP-Mg(2-)) was the apparent substrate for spinach ribulose bisphosphate carboxylase/oxygenase. The apparent Km for total RuBP (pH 8.0 at 30° C) increased with increasing Mg(2+) concentrations from 11.6 μM at 13.33 mM Mg(2+) to 32.6 μM at 40.33 mM Mg(2+). Similarly the apparent Km for RuBP-Mg(2-) complex increased with increasing Mg(2+) from 9.4 μM at 13.33 mM Mg(2+) to 29.7 μM at 40.33 mM Mg(2+). However, the Km values for uncomplexed RuBP(4-) were independent of the (saturating) concentration of Mg(2+) (Km=2.2 μM). The Vmax did not vary with the changing concentrations of Mg(2+).In contrast, the Km for total RuBP remained constant with varying Mg(2+) concentrations (Km=59.5 μM) for the enzyme from R. rubrum. The apparent Km for the RuBP-Mg(2-) complex decreased with increasing Mg(2+) concentrations from 16.0 μM at 7.5 mM Mg(2+) to 5.9 μM at 27.5 mM Mg(2+). The initial velocity for the C. vinosum enzyme was also found to be independent of the (saturating) concentration of Mg(2+) when total RuBP was varied in the assay. Thus the response to total RuBP by these two bacterial enzymes, which markedly differ in structure, was closely similar.
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