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DOI 10.1046/j.1365-2672.2000.01117.x

Медицинская библиотека · Journal of applied microbiology · 2000

Production of rhodanese by bacteria present in bio-oxidation plants used to recover gold from arsenopyrite concentrates.

Gardner M N, Rawlings D E

СтатьяПоддержка исследования: вне правительства СШАПеревод в очереди

Аннотация

Considerably larger quantities of cyanide are required to solubilize gold following the bio-oxidation of gold-bearing ores compared with oxidation by physical-chemical processes. A possible cause of this excessive cyanide consumption is the presence of the enzyme rhodanese. Rhodanese activities were determined for the bacteria most commonly encountered in bio-oxidation tanks. Activities of between 6.4 and 8.2 micromol SCN min(-1) mg protein(-1) were obtained for crude enzyme extracts of Thiobacillus ferrooxidans, Thiobacillus thiooxidans and Thiobacillus caldus, but no rhodanese activity was detected in Leptospirillum ferrooxidans. Rhodanese activities 2-2.5-fold higher were found in the total mixed cell mass from a bio-oxidation plant. T. ferrooxidans synthesized rhodanese irrespective of whether it was grown on iron or sulphur. With a PCR-based detection technique, only L. ferrooxidans and T. caldus cells were detected in the bio-oxidation tanks. As no rhodanese activity was associated with L. ferrooxidans, it was concluded that T. caldus was responsible for all of the rhodanese activity. Production of rhodanese by T. caldus in batch culture was growth phase-dependent and highest during early stationary phase. Although the sulphur-oxidizing bacteria were clearly able to convert cyanide to thiocyanate, it is unlikely that this rhodanese activity is responsible for the excessive cyanide wastage at the high pH values associated with the gold solubilization process.

Для цитирования: Gardner M N, Rawlings D E. Production of rhodanese by bacteria present in bio-oxidation plants used to recover gold from arsenopyrite concentrates.. Journal of applied microbiology. 2000. DOI: 10.1046/j.1365-2672.2000.01117.x.

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