SOLUBILIZATION OF CU2-OXIDIZING BACTERIA ISOLATED FROM THE NATURAL-ENVIRONMENT AND IDENTIFICATION OF THE ENZYME THAT DETERMINES CU2+ SOLUBILIZATION ACTIVITY( FROM COPPER ORE BY IRON)
T. Sugio et F. Akhter, SOLUBILIZATION OF CU2-OXIDIZING BACTERIA ISOLATED FROM THE NATURAL-ENVIRONMENT AND IDENTIFICATION OF THE ENZYME THAT DETERMINES CU2+ SOLUBILIZATION ACTIVITY( FROM COPPER ORE BY IRON), Journal of fermentation and bioengineering, 82(4), 1996, pp. 346-350
Solubilization of Cu2+ from copper concentrate by 67 strains of iron-o
xidizing bacteria isolated from the natural environment was studied. I
n the case of static growth on copper concentrate (5%)-salt medium (pH
2.5) at 30 degrees C, Cu2+ solubilization activities of 65 strains in
cluding Thiobacillus ferrooxidans strains AP19-3, OK-2, OK-3, OK1-50,
Funis and NASF-1 ranged from 2.5-3.5 mg Cu2+/ml/33 d. in contrast, the
activities of T. ferrooxidans strains KO-1 and NA-1 were quite low at
0.9 mg Cu2+/ml/33 d. Nonbiological solubilization activity of Cu2+ wa
s 0.4 mg Cu2+/ml/33 d. For identification of the enzymes that play a c
rucial role in biological Cu2+ solubilization, the activities of the e
nzymes involved in iron and sulfur oxidations were compared among the
strains described above. No significant differences in the growth on i
ron-salt medium and the levels of cellular iron oxidizing activity wer
e observed, In contrast, a marked difference was observed in the cellu
lar activity of an enzyme that was involved in the first step of sulfu
r oxidation in T. ferrooxidans, i.e., hydrogen sulfide: ferric ion oxi
doreductase (SFORase). Strains Funis, OK1-50, NASF-1, OK-3, AP19-3, OK
-2 which showed high Cu2+ solubilization activity showed high SFORase
activity (1.3-4.0 mu mol Fe2+/ml/4 h). In contrast, strains NA-1 and K
O-1 which showed low Cu2+ solubilization activity showed low SFORase a
ctivity (0.3-0.4 mu mol Fe2+/ml/4 h), suggesting that SFORase, but not
iron oxidase, is the enzyme that determines the ability of T. ferroox
idans to solubilize Cu2+ from copper concentrate.