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61.
Chardin B. Gallice P. Sari J. C. Bruschi M. 《Journal of Thermal Analysis and Calorimetry》2002,70(2):475-482
The effect of Cr(VI) on Desulfovibrio vulgaris strain Hildenborough bioenergetic metabolism was monitored by microcalorimetry and the concomitant reduction of this metal
was studied. Results showed that Cr(VI) is reduced by the bacterium and that the bacterial growth is altered, involving a
strong modification of the metabolism of the bacteria. An absence of correlation between Cr(VI) reduction and cell growth
is observed, suggesting that Cr(VI) does not yield energy to support anaerobic growth. The analysis of the enzymatic characteristics
of Cr(VI) reduction are in progress.
This revised version was published online in August 2006 with corrections to the Cover Date. 相似文献
62.
报道了趋磁细菌WD-1生长和磁小体合成的最适条件。在pH6.7、28℃和静止培养条件下,每100mL含50~100mg柠檬酸或100~150mgα-酮戊二酸和20mg硫酸铵分别是WD-1生长的最适碳、氮源,碳氮比以5:1或4:1为好。每100mL含50mg柠檬酸、75~125mgα-酮戊二酸、75mg酒石酸或175mg乙酸钠,10mg硝酸钠或10~20mg硫酸铵,15μmol·L~(-1)三氯化铁或硫酸亚铁分别是磁小体合成的最适碳、氮和铁源。而1~3%的氧浓度是必需的。 相似文献
63.
Affinity purification of metalloprotease from marine bacterium using immobilized metal affinity chromatography 下载免费PDF全文
Juan Yang Jing Bao Junzhong Liu Shengxiang Lin Mi Sun 《Journal of separation science》2016,39(11):2050-2056
In this study, an efficient affinity purification protocol for an alkaline metalloprotease from marine bacterium was developed using immobilized metal affinity chromatography. After screening and optimization of the affinity ligands and spacer arm lengths, Cu‐iminmodiacetic acid was chosen as the optimal affinity ligand, which was coupled to Sepharose 6B via a 14‐atom spacer arm. The absorption analysis of this medium revealed a desorption constant Kd of 21.5 μg/mL and a theoretical maximum absorption Qmax of 24.9 mg/g. Thanks to this affinity medium, the enzyme could be purified by only one affinity purification step with a purity of approximately 95% pure when analyzed by high‐performance liquid chromatography and reducing sodium dodecyl sulfate polyacrylamide gel electrophoresis. The recovery of the protease activity reached 74.6%, which is much higher than the value obtained by traditional protocols (8.9%). These results contribute to the industrial purifications and contribute a significant reference for the purification of other metalloproteases. 相似文献