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球形红细菌厌氧降解2,4-二硝基甲苯 总被引:2,自引:0,他引:2
【目的】研究不同环境条件对2,4-二硝基甲苯(2,4-DNT)生物降解的影响。【方法】采用光合细菌球形红细菌在温度为30 °C的光照培养箱中厌氧降解2,4-DNT,并用高效液相色谱仪测定其浓度。【结果】去除2,4-DNT的最佳条件是初始浓度40 mg/L、初始pH 7.0和接种量15%。另外,2,4-DNT在菌体延滞期被细胞吸收,然后在指数期作为碳源被降解。2,4-DNT的去除率在72 h达到98.8%。从液相色谱图中观察到有2种中间代谢产物,但在120 h内产物被逐渐降解。2,4-DNT的去除动力学符合一级速率模型。【结论】不同条件下2,4-DNT的去除率表明球形红细菌能有效降解2,4-DNT。 相似文献
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Non-reciprocal regulation of Rhodobacter capsulatus and Rhodobacter sphaeroides recA genes expression 总被引:1,自引:0,他引:1
Antonio R.Fernandez de Henestrosa Eusebi Rivera Jordi Barbé 《FEMS microbiology letters》1995,129(2-3):175-181
Abstract The Rhodobacter capsulatus recA gene has been isolated and sequenced. Its deduced amino acid sequence showed the closest identity with the Rhodobacter sphaeroides RecA protein (91% identity). However, the promoter regions of both R. capsulatus and R. sphaeroides recA genes are only 64% similar. An Escherichia coli -like LexA binding site was not present in the upstream region of the R. capsulatus recA gene. Nevertheless, the R. capsulatus recA gene is inducible by DNA damage in both hetero- and phototrophically growing conditions. The R. capsulatus recA gene is poorly induced when inserted into the chromosome of R. sphaeroides , indicating that the recA gene of both bacteria possess different control sequences despite their phylogenetically close relationship. 相似文献
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从淀粉废水中分离获得一株光合细菌,经形态特征,培养特征,生理生化特征及G+Cmol%含量等生物学特性分析,确定为球形红杆菌(Rhodobactersphaeroides)L2。该菌应用于淀粉废水处理,COD去除率达95.7%发酵产类胡萝卜素,产量达295mg/L;作为饲料添加剂进行肉鸡饲喂,增重16.40%。 相似文献
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B B Nepple J Kessi R Bachofen 《Journal of industrial microbiology & biotechnology》2000,25(4):198-203
Rhodobacter sphaeroides grew in the presence of up to 43 μM chromate and reduced hexavalent chromium to the trivalent form under both aerobic and
anaerobic conditions. Reduced chromium remained in the external medium. Reductase activity was present in cells of R. sphaeroides independent of whether chromate was present or not in the growth medium. The reducing activity was found in the cytoplasmic
cell fraction and was dependent on NADH. The chromate-reducing enzyme was purified by anion exchange, hydroxyapatite and hydrophobic
interaction chromatography, and gel filtration. The molecular weight of the enzyme was 42 kDa as determined by gel filtration.
The optimum of the reaction is at pH 7.0 and 30°C. The enzyme activity showed a hyperbolic dependence on the concentrations
of both substrates, NADH and chromate, with a maximum velocity at 0.15 mM NADH. A K
m of 15±1.3 μM CrO4
2− and a V
max of 420±50 μmol min−1 mg protein−1 was determined for the enzyme isolated from anaerobically grown cells and 29±6.4 μM CrO4
2− and 100±9.6 μmol CrO4
2− min−1 mg protein−1 for the one from aerobically grown ones. Journal of Industrial Microbiology & Biotechnology (2000) 25, 198–203.
Received 05 January 2000/ Accepted in revised form 27 May 2000 相似文献
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Stephen J. Wagner S. Edward Stevens Jr. B. Tracey Nixon David H. Lambert Robert G. Quivey Jr. F. Robert Tabita 《FEMS microbiology letters》1988,55(2):217-222
The nucleotide sequence for the Rhodobacter sphaeroides form II ribulose 1,5-bisphosphate carboxylase/oxygenase was determined. The deduced product is highly homologous with the form II-like enzyme of Rhodospirillum rubrum , but appears to be more distantly related to the large subunit of the L8 S8 enzyme found in autotrophic bacteria, cyanobacteria and higher plants. Several regions highly conserved among L8 S8 and LX enzymes correspond with regions previously implicated in catalytic activity and subunit interactions. An imperfect palindrome and a stem loop structure were identified in the 5' and 3' flanking sequences, respectively, of R. sphaeroides rbpL . 相似文献
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A protein closely related to the Escherichia coli GroEL protein has been isolated from Rhodobacter sphaeroides. Native and SDS-polyacrylamide gel electrophoresis of this protein have shown that it is present in the cell as a multimeric complex of Mr 670,000 which is composed of a monomer of Mr 58,000. Antisera raised against the Mr 58,000 polypeptide have been shown to cross-react with GroEL and the alpha subunit of the pea plastid chaperonin. The N-terminal amino acid sequence of the Mr 58,000 polypeptide is identical to that of GroEL at 15 of 19 residues and is also closely related to the alpha subunit of the pea plastid chaperonin, though less so to the beta subunit. 相似文献