Kinetic development and evaluation of membrane sequencing batch reactor (MSBR) with mixed cultures photosynthetic bacteria for dairy wastewater treatment.

This experimental study was conducted to evaluate a membrane sequencing batch reactor (MSBR) with mixed culture photosynthetic bacteria for dairy wastewater treatment. The study was undertaken in two steps: laboratory and pilot scale experiments. In the first step, kinetics analysis of the MSBR was carried out in a laboratory scale experiment with influent COD concentration of 2500 mg/L. The pilot scale experiment was conducted to investigate the performance of the MSBR and checked the suitability of the kinetics for an engineering design. The kinetic coefficients K(s), k, k(d), Y and mu(m) were found to be 174-mg-COD/L, 7.42/d, 0.1383/d, 0.2281/d and 1.69/d, respectively. There were some deviations of COD removal efficiency between the design value and the actual value. From the kinetics estimation, COD effluent from the design was 27 mg/L while the average actual COD effluent from the experiment was 149 mg/L. Due to the different light source condition, the factors relating to light energy (i.e. L(f) and IR(%)) must be incorporated into engineering design and performance prediction with these kinetic coefficients of the photosynthetic MSBR.

Nutrient optimization for production of polyhydroxybutyrate from halotolerant photosynthetic bacteria cultivated under aerobic-dark condition

Three halotolerant bacterial strains; Rhodobacter sphaeroides ES16 (the wild type) and the two mutant strains of R. sphaeroides ES16, namely N20 and U7, were cultivated in glutamate-malate (GM) medium and screened for production of polyhydroxybutyrate (PHB). The mutant strains N20 and U7 were found to accumulate PHB (53.9 and 42.0 percent of DCW, respectively) 3.6 and 2.8 times higher than the wild type strain (19.5 percent of DCW), respectively. R. sphaeroides N20 were selected for studies on the effects of nutrient and environmental conditions on PHB accumulation. The optimal condition was 4 g/l acetate, 0.02 g/l (NH4)2SO4, C/N ratio of 6:1, 1.0 g/l K2HPO4, 1.0 g/l KH2PO4 and 3 percent NaCl with initial pH at 7.0. Under this optimal condition, the maximum PHB accumulation increased from 53.9 percent to 88 percent of DCW and 9.11 ± 0.08 g/l biomass, 8.02 +/- 0.10 g/l PHB concentration were achieved after 60 hrs cultivation at 37ºC. These results are the highest values ever obtained from photosynthetic bacteria reported so far.

Photosynthetic apparatus of antenna-reaction centres supercomplexes in oxyphotobacteria: insight through significance of Pcb/IsiA proteins.

In this Review we give an overview of the structure and function of the membrane-bound photosynthetic antenna reaction centre complexes present in oxyphotobacteria. We summarise how variations in the organisation of these complexes have enabled oxyphotobacteria to exploit different ecological niches and discuss the evolutionary relationships of the IsiA/Pcb family of pigment-binding proteins.

Regulation of glutamine synthetase by metal-catalyzed oxidative modification in the marine oxyphotobacterium Prochlorococcus.

The inactivation of glutamine synthetase (GS; EC 6.3.1.2) by metal-catalyzed oxidation (MCO) systems was studied in several Prochlorococcus strains, including the axenic PCC 9511. GS was inactivated in the presence of various oxidative systems, either enzymatic (as NAD(P)H+NAD(P)H-oxidase+Fe(3+)+O(2)) or non-enzymatic (as ascorbate+Fe(3+)+O(2)). This process required the presence of oxygen and a metal cation, and is prevented under anaerobic conditions. Catalase and peroxidase, but not superoxide dismutase, effectively protected the enzyme against inactivation, suggesting that hydrogen peroxide mediates this mechanism, although it is not directly responsible for the reaction. Addition of azide (an inhibitor of both catalase and peroxidase) to the MCO systems enhanced the inactivation. Different thiols induced the inactivation of the enzyme, even in the absence of added metals. However, this inactivation could not be reverted by addition of strong oxidants, as hydrogen peroxide or oxidized glutathione. After studying the effect of addition of the physiological substrates and products of GS on the inactivation mechanism, we could detect a protective effect in the case of inorganic phosphate and glutamine. Immunochemical determinations showed that the concentration of GS protein significantly decreased by effect of the MCO systems, indicating that inactivation precedes the degradation of the enzyme.

Structure and function of the cytochrome bc1 complex of mitochondria and photosynthetic bacteria.

Progress has recently been made in the understanding of the function of the cytochrome bc1 complex and related proteins in the context of recent structural information. The structures support many features that were predicted from sequence analysis and biophysical studies, but contain some surprises. Most dramatically, it is apparent that the iron-sulfur protein can take up different positions in different crystals, suggesting a novel mechanism for electron transfer through domain movement. Evidence from studies of mutant strains, in which the function of the sites or the binding of inhibitors is perturbed, has provided clues about the mechanism.