scholarly journals Production of trimethylamine from structurally related trimethylammonium compounds by resting cell suspensions of ?-butyrobetaine-and d, l-carnitine-grown Acinetobacter calcoaceticus and Pseudomonas putida

1984 ◽  
Vol 137 (1) ◽  
pp. 88-88
Author(s):  
Sasha Englard ◽  
John S. Blanchard ◽  
Judy Miura-Fraboni
Keyword(s):  
Pseudomonas Putida ◽  
Acinetobacter Calcoaceticus ◽  
Cell Suspensions ◽  
Resting Cell

Assimilation of ?-butyrobetaine, and d-and l-carnitine by resting cell suspensions of Acinetobacter calcoaceticus and Pseudomonas putida

1982 ◽  
Vol 133 (3) ◽  
pp. 217-221 ◽  
Author(s):  
Judy Miura-Fraboni ◽  
Hans-Peter Kleber ◽  
Sasha Englard
Keyword(s):  
Pseudomonas Putida ◽  
Acinetobacter Calcoaceticus ◽  
Cell Suspensions ◽  
Resting Cell

scholarly journals Analysis of Dibenzothiophene Desulfurization in a Recombinant Pseudomonas putida Strain

2008 ◽  
Vol 75 (3) ◽  
pp. 875-877 ◽  
Author(s):  
Javier Calzada ◽  
Mar�a T. Zamarro ◽  
Almudena Alc�n ◽  
Victoria E. Santos ◽  
Eduardo D�az ◽  
...  
Keyword(s):  
Pseudomonas Putida ◽  
Exponential Growth ◽  
Exponential Phase ◽  
Cell Process ◽  
Growth Phases ◽  
Early Exponential Phase ◽  
Sharp Maximum ◽  
Resting Cell

ABSTRACT Biodesulfurization was monitored in a recombinant Pseudomonas putida CECT5279 strain. DszB desulfinase activity reached a sharp maximum at the early exponential phase, but it rapidly decreased at later growth phases. A model two-step resting-cell process combining sequentially P. putida cells from the late and early exponential growth phases was designed to significantly increase biodesulfurization.

Influence of External pH on Alkaloid Production and Excretion by Catharanthus Roseus Resting Cell Suspensions

1987 ◽  
pp. 529-533
Author(s):  
Claudine Nef ◽  
Christian Ambid ◽  
Jean Fallot
Keyword(s):  
Catharanthus Roseus ◽  
Cell Suspensions ◽  
Alkaloid Production ◽  
Resting Cell ◽  
External Ph

Products of anaerobic phloroglucinol degradation by Coprococcus sp. Pe15

1976 ◽  
Vol 22 (2) ◽  
pp. 159-164 ◽  
Author(s):  
Chii-Guary Tsai ◽  
Diane M. Gates ◽  
W. M. Ingledew ◽  
G. A. Jones
Keyword(s):  
Carbon Dioxide ◽  
Acetic Acid ◽  
Rumen Fluid ◽  
Cell Suspensions ◽  
Anaerobic Conditions ◽  
Fluid Medium ◽  
Resting Cell ◽  
Flavonoid Compounds

Under anaerobic conditions, resting cell suspensions of Coprococcus sp. Pe15 degraded 1 molecule of phloroglucinol to 2 molecules of acetic acid and 2 molecules of carbon dioxide. The organism metabolized the flavonoids rhamnetin and quercetin anaerobically in 20% rumen fluid medium but failed to grow under similar conditions at the expense of any of 39 other aromatic or flavonoid compounds tested.

scholarly journals Microbially Mediated Biodegradation of Hexahydro-1,3,5-Trinitro-1,3,5- Triazine by Extracellular Electron Shuttling Compounds

2006 ◽  
Vol 72 (9) ◽  
pp. 5933-5941 ◽  
Author(s):  
Man Jae Kwon ◽  
Kevin T. Finneran
Keyword(s):  
Humic Substances ◽  
Electron Donor ◽  
Cell Suspensions ◽  
Electron Shuttle ◽  
Geobacter Metallireducens ◽  
Electron Shuttling ◽  
Resting Cell ◽  
Molar Basis ◽  
Novel Approach

ABSTRACT The potential for humic substances to stimulate the reduction of hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) was investigated. This study describes a novel approach for the remediation of RDX-contaminated environments using microbially mediated electron shuttling. Incubations without cells demonstrated that reduced AQDS transfers electrons directly to RDX, which was reduced without significant accumulation of the nitroso intermediates. Three times as much reduced AQDS (molar basis) was needed to completely reduce RDX. The rate and extent of RDX reduction differed greatly among electron shuttle/acceptor amendments for resting cell suspensions of Geobacter metallireducens and G. sulfurreducens with acetate as the sole electron donor. AQDS and purified humic substances stimulated the fastest rate of RDX reduction. The nitroso metabolites did not significantly accumulate in the presence of AQDS or humic substances. RDX reduction in the presence of poorly crystalline Fe(III) was relatively slow and metabolites transiently accumulated. However, adding humic substances or AQDS to Fe(III)-containing incubations increased the reduction rates. Cells of G. metallireducens alone reduced RDX; however, the rate of RDX reduction was slow relative to AQDS-amended incubations. These data suggest that extracellular electron shuttle-mediated RDX transformation is not organism specific but rather is catalyzed by multiple Fe(III)- and humic-reducing species. Electron shuttle-mediated RDX reduction may eventually become a rapid and effective cleanup strategy in both Fe(III)-rich and Fe(III)-poor environments.

scholarly journals Characterization of Hybrid Toluate and Benzoate Dioxygenases

2003 ◽  
Vol 185 (18) ◽  
pp. 5333-5341 ◽  
Author(s):  
Yong Ge ◽  
Lindsay D. Eltis
Keyword(s):  
Substrate Specificity ◽  
Pseudomonas Putida ◽  
Acinetobacter Calcoaceticus ◽  
The Other ◽  
Β Subunit ◽  
Structural Determinants ◽  
Α Subunit ◽  
Benzoate Dioxygenase

ABSTRACT Toluate dioxygenase of Pseudomonas putida mt-2 (TADOmt2) and benzoate dioxygenase of Acinetobacter calcoaceticus ADP1 (BADOADP1) catalyze the 1,2-dihydroxylation of different ranges of benzoates. The catalytic component of these enzymes is an oxygenase consisting of two subunits. To investigate the structural determinants of substrate specificity in these ring-hydroxylating dioxygenases, hybrid oxygenases consisting of the α subunit of one enzyme and the β subunit of the other were prepared, and their respective specificities were compared to those of the parent enzymes. Reconstituted BADOADP1 utilized four of the seven tested benzoates in the following order of apparent specificity: benzoate > 3-methylbenzoate > 3-chlorobenzoate > 2-methylbenzoate. This is a significantly narrower apparent specificity than for TADOmt2 (3-methylbenzoate > benzoate ∼ 3-chlorobenzoate > 4-methylbenzoate ∼ 4-chlorobenzoate ≫ 2-methylbenzoate ∼ 2-chlorobenzoate [Y. Ge, F. H. Vaillancourt, N. Y. Agar, and L. D. Eltis, J. Bacteriol. 184:4096-4103, 2002]). The apparent substrate specificity of the αBβT hybrid oxygenase for these benzoates corresponded to that of BADOADP1, the parent from which the α subunit originated. In contrast, the apparent substrate specificity of the αTβB hybrid oxygenase differed slightly from that of TADOmt2 (3-chlorobenzoate > 3-methylbenzoate > benzoate ∼ 4-methylbenzoate > 4-chlorobenzoate > 2-methylbenzoate > 2-chlorobenzoate). Moreover, the αTβB hybrid catalyzed the 1,6-dihydroxylation of 2-methylbenzoate, not the 1,2-dihydroxylation catalyzed by the TADOmt2 parent. Finally, the turnover of this ortho-substituted benzoate was much better coupled to O2 utilization in the hybrid than in the parent. Overall, these results support the notion that the α subunit harbors the principal determinants of specificity in ring-hydroxylating dioxygenases. However, they also demonstrate that the β subunit contributes significantly to the enzyme's function.

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