Immobilization of Desulfovibrio vulgaris cells with hydrogenase activity

2007 ◽  
Vol 50 (4) ◽  
pp. 563-570 ◽  
Author(s):  
M. C. Barreto ◽  
J. M. S. Cabral
1987 ◽  
Vol 53 (7) ◽  
pp. 1708-1710 ◽  
Author(s):  
C Chatelus ◽  
P Carrier ◽  
P Saignes ◽  
M F Libert ◽  
Y Berlier ◽  
...  

1998 ◽  
Vol 180 (6) ◽  
pp. 1460-1465 ◽  
Author(s):  
Gabor Rakhely ◽  
Annette Colbeau ◽  
Jerome Garin ◽  
Paulette M. Vignais ◽  
Kornel L. Kovacs

ABSTRACT The characterization of a hyd gene cluster encoding the stable, bidirectional [NiFe]hydrogenase 1 enzyme in Thiocapsa roseopersicina BBS, a purple sulfur photosynthetic bacterium belonging to the family Chromatiaceae, is presented. The heterodimeric hydrogenase 1 had been purified to homogeneity and thoroughly characterized (K. L. Kovacs et al., J. Biol. Chem. 266:947–951, 1991; C. Bagyinka et al., J. Am. Chem. Soc. 115:3567–3585, 1993). As an unusual feature, a 1,979-bp intergenic sequence (IS) separates the structural geneshydS and hydL, which encode the small and the large subunits, respectively. This IS harbors two sequential open reading frames (ORFs) which may code for electron transfer proteins ISP1 and ISP2. ISP1 and ISP2 are homologous to ORF5 and ORF6 in thehmc operon, coding for a transmembrane electron transfer complex in Desulfovibrio vulgaris. Other accessory proteins are not found immediately downstream or upstream of hydSL. A hup gene cluster coding for a typical hydrogen uptake [NiFe]hydrogenase in T. roseopersicina was reported earlier (A. Colbeau et al. Gene 140:25–31, 1994). The deduced amino acid sequences of the two small (hupS andhydS) and large subunit (hupL andhydL) sequences share 46 and 58% identity, respectively. The hup and hyd genes differ in the arrangement of accessory genes, and the genes encoding the two enzymes are located at least 15 kb apart on the chromosome. Both hydrogenases are associated with the photosynthetic membrane. A stable and an unstable hydrogenase activity can be detected in cells grown under nitrogen-fixing conditions; the latter activity is missing in cells supplied with ammonia as the nitrogen source. The apparently constitutive and stable activity corresponds to hydrogenase 1, coded byhydSL, and the inducible and unstable second hydrogenase may be the product of the hup gene cluster.


1995 ◽  
Vol 96 (3) ◽  
pp. 329-333 ◽  
Author(s):  
Toshiaki Kamachi ◽  
Seiichi Uno ◽  
Tomohiro Hiraishi ◽  
Ichiro Okura

2019 ◽  
Vol 26 (2) ◽  
pp. 63-71
Author(s):  
Ling Leng ◽  
Ying Wang ◽  
Peixian Yang ◽  
Takashi Narihiro ◽  
Masaru Konishi Nobu ◽  
...  

Chain elongation of volatile fatty acids for medium chain fatty acids production (e.g. caproate) is an attractive approach to treat wastewater anaerobically and recover resource simultaneously. Undefined microbial consortia can be tailored to achieve chain elongation process with selective enrichment from anaerobic digestion sludge, which has advantages over pure culture approach for cost-efficient application. Whilst the metabolic pathway of the dominant caproate producer, Clostridium kluyveri, has been annotated, the role of other coexisting abundant microbiomes remained unclear. To this end, an ethanol-acetate fermentation inoculated with fresh digestion sludge at optimal conditions was conducted. Also, physiological study, thermodynamics and 16 S rRNA gene sequencing to elucidate the biological process by linking the system performance and dominant microbiomes were integrated. Results revealed a possible synergistic network in which C. kluyveri and three co-dominant species, Desulfovibrio vulgaris, Fusobacterium varium and Acetoanaerobium sticklandii coexisted. D. vulgaris and A. sticklandii (F. varium) were likely to boost the carboxylates chain elongation by stimulating ethanol oxidation and butyrate production through a syntrophic partnership with hydrogen (H2) serving as an electron messenger. This study unveils a synergistic microbial network to boost caproate production in mixed culture carboxylates chain elongation.


1965 ◽  
Vol 48 (2) ◽  
pp. 263-271 ◽  
Author(s):  
Herbert Schriefers ◽  
Gerlinde Scharlau ◽  
Franzis Pohl

ABSTRACT After the administration of anabolic steroids to adult female rats in daily doses of 1 mg per animal for 14 days, the following parameters were investigated: the rate of the Δ4-5α-hydrogenase-catalyzed cortisone reduction in liver slices and microsomal fractions, the adrenal weight and the in vitro corticosterone production rate. Among the steroids tested, only 17α-methyl-testosterone and 17α-ethyl-19-nor-testosterone were effective in lowering significantly cortisone reduction rate by liver slices with concomitant decreases in microsomal Δ4-5α-hydrogenase-activity. Testosterone, 19-nor-testosterone, 17α-ethinyl-19-nor-testosterone, 17α-methyl-17β-hydroxy-androsta-1,4-dien-3-one and 1-methyl-17β-hydroxy-androst-1-en-3-one were ineffective or only slightly effective. Adrenal weight and absolute corticosterone production rate (μg/60 min per animal) were decreased after treatment with 17α-methyl-testosterone, 17α-ethyl-19-nor-testosterone and 1-methyl-17β-hydroxy-androst-1-en-3-one. Corticosterone production was decreased with 17α-ethinyl-19-nor-testosterone in spite of an unchanged adrenal weight. The relative corticosterone production rate (μg/60 min · 100 mg adrenal) was in any cases unaffected. According to these results there exists – with the exception of 17α-ethinyl-19-nor-testosterone – a strict parallelism between corticosteroid turnover and corticosterone production rate: unchanged turnover is correlated with unchanged corticosterone production rate, while a decreased turnover is correlated with decreased adrenal activity. The protein-anabolic effect of certain anabolic steroids may be partly due to an anti-catabolic action of these compounds resulting from a decreased corticosteroid inactivation and production rate. Possible mechanisms by which anabolic steroids may affect corticosteroid-balance are discussed.


1997 ◽  
Vol 36 (6-7) ◽  
pp. 383-390 ◽  
Author(s):  
J. E. Teer ◽  
D. J. Leak ◽  
A. W. L. Dudeney ◽  
A. Narayanan ◽  
D. C. Stuckey

The presence of small amounts of iron (>0.013% Fe) in sand creates problems in the manufacture of high quality glass. Removal by hot sulphuric acid is possible, but creates environmental problems, and is costly. Hence organic acids such as oxalic have been investigated since they are effective in removing iron, and can be degraded anaerobically. The aim of this work was to identify key intermediates in the anaerobic degradation of oxalate in an upflow anaerobic sludge blanket reactor (UASB) which was removing iron from solution in the sulphide form, and to determine the bacterial species involved. 2-bromoethanesulfonic acid (BES) and molybdenum were selected as suitable inhibitors for methanogenic and sulphate reducing bacteria (SRB) respectively. 40mM molybdenum was used to inhibit the SRB in a reactor with a 12hr HRT. Total SRB inhibition took place in 20 hrs, with a complete breakthrough of influent sulphate. The lack of an immediate oxalate breakthrough confirmed Desulfovibrio vulgaris subspecies oxamicus was not the predominant oxalate utilising species. Nevertheless, high concentrations of molybdenum were found to inhibit oxalate utilising bacteria in granular reactors but not in suspended population reactors; this observation was puzzling, and at present cannot be explained. Based on the intermediates identified, it was postulated that oxalate was degraded to formate by an oxalate utilising bacteria such as Oxalobacter formigenes, and the formate used by the SRBs to reduce sulphate. Acetate, as a minor intermediate, existed primarily as a source of cell carbon for oxalate utilising bacteria. Methanogenic inhibition identified that 62% of the CH4 in the reactor operated at 37°C originated from hydrogenotrophic methanogenesis, whilst this figure was 80% at 20°C. Possible irreversible effects were recorded with hydrogenotrophic methanogens.


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